|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
22-597 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 712.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 22 AKNTKGTVMRVWNYMGYQKAALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQ 101
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 102 IFVMVNVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDW 181
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 182 ILAIVTLITVPIMFFVTKKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKAD 261
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 262 TFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEIMDEV 341
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 342 PEIKNKKDAFVVQNLQGHVALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDG 421
Cdd:COG1132 322 PEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 422 KNIKEYDINSLRGKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQ 501
Cdd:COG1132 402 VDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQ 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 502 KQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKGNHESL 581
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
570
....*....|....*.
gi 1267510758 582 MEDRGFYFDLYTSQFK 597
Cdd:COG1132 562 LARGGLYARLYRLQFG 577
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
21-595 |
1.43e-171 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 504.37 E-value: 1.43e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 21 KAKNTKGTVMRVWNYMGYQKAALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWL 100
Cdd:COG2274 136 KRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 101 QIFVMVNVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALD 180
Cdd:COG2274 216 RSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYS 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 181 WILAIVTLITVPIM----FFVTKKLVAYSgknfAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVS 256
Cdd:COG2274 295 PPLALVVLLLIPLYvllgLLFQPRLRRLS----REESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 257 ATKADTFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFE 336
Cdd:COG2274 371 RFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDD 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 337 IMDEVPEIKNKKDAFVVQNLQGHVALENVSFGYEENKT-ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQG 415
Cdd:COG2274 451 ILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDSPpVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSG 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 416 QIHIDGKNIKEYDINSLRGKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGS 495
Cdd:COG2274 531 RILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGS 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 496 NLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEK 575
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
570 580
....*....|....*....|
gi 1267510758 576 GNHESLMEDRGFYFDLYTSQ 595
Cdd:COG2274 691 GTHEELLARKGLYAELVQQQ 710
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
28-597 |
6.62e-142 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 423.36 E-value: 6.62e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 28 TVMRVWNYMGYQK-----AALTFVIFLVFVTTLLGLLGPylmgvIIDQYIVPKDLSGTARMCLLLIAI--------YGVT 94
Cdd:TIGR02203 1 TFRRLWSYVRPYKaglvlAGVAMILVAATESTLAALLKP-----LLDDGFGGRDRSVLWWVPLVVIGLavlrgicsFVST 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 95 VFLTWlqifvmvnVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTI 174
Cdd:TIGR02203 76 YLLSW--------VSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 175 AMFALDWILAIVTLITVPI----MFFVTKKLVAYSgknfAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKIN 250
Cdd:TIGR02203 148 VLLYYSWQLTLIVVVMLPVlsilMRRVSKRLRRIS----KEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 251 EQLRVSATKADTFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAG 330
Cdd:TIGR02203 224 NRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 331 GERVFEIMDEVPEIKNKKDAfvVQNLQGHVALENVSFGY-EENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRF 409
Cdd:TIGR02203 304 AESLFTLLDSPPEKDTGTRA--IERARGDVEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 410 YDIQQGQIHIDGKNIKEYDINSLRGKIGVVLQDTYLFAGTIMDNIRYGRL-DASDEEVINAAKAASAHSFIKHLPNQYET 488
Cdd:TIGR02203 382 YEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDT 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 489 KIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIK 568
Cdd:TIGR02203 462 PIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMD 541
|
570 580
....*....|....*....|....*....
gi 1267510758 569 DGSIIEKGNHESLMEDRGFYFDLYTSQFK 597
Cdd:TIGR02203 542 DGRIVERGTHNELLARNGLYAQLHNMQFR 570
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
33-595 |
9.02e-132 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 398.42 E-value: 9.02e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 33 WNYMGYQKAALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTArmcLLLIAIYGV----TVFLTWLQIFVMVNV 108
Cdd:COG5265 29 PPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVP---VGLLLAYGLlrllSVLFGELRDALFARV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 109 ALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDL---MSRVTNDIDNLnqaLTQSVVQIISSALTFIGVTIAMFAL-DWILA 184
Cdd:COG5265 106 TQRAVRRLALEVFRHLHALSLRFHLERQTGGLsrdIERGTKGIEFL---LRFLLFNILPTLLEIALVAGILLVKyDWWFA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 185 IVTLITVpimffvtkklVAYSGKNFA---KRQKDLGELNGFIEEAITGAdVTTL--YgkekETVQNFNkiNE-------- 251
Cdd:COG5265 183 LITLVTV----------VLYIAFTVVvteWRTKFRREMNEADSEANTRA-VDSLlnY----ETVKYFG--NEarearryd 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 252 ----QLRVSATKADTfsafifpSMNFINnLGMGLVIGTGSVMVLnGMTTVGVIA--------AFIN-YSRQFSRPLSQFA 318
Cdd:COG5265 246 ealaRYERAAVKSQT-------SLALLN-FGQALIIALGLTAMM-LMAAQGVVAgtmtvgdfVLVNaYLIQLYIPLNFLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 319 TLMNTIQAAVAGGERVFEIMDEVPEIKNKKDAFVVQNLQGHVALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSG 398
Cdd:COG5265 317 FVYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 399 KTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSF 478
Cdd:COG5265 397 KSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 479 IKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTI 558
Cdd:COG5265 477 IESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTI 556
|
570 580 590
....*....|....*....|....*....|....*..
gi 1267510758 559 EKADQILVIKDGSIIEKGNHESLMEDRGFYFDLYTSQ 595
Cdd:COG5265 557 VDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
43-334 |
2.04e-126 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 373.66 E-value: 2.04e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 43 LTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPK------DLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKI 116
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLgggggvDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 117 RQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFF 196
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 197 VTKKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINN 276
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 277 LGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18547 241 LGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
31-586 |
2.69e-126 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 382.95 E-value: 2.69e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 31 RVWNYMGYQKAALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPK-DLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVA 109
Cdd:COG4988 7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGaPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 110 LKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLI 189
Cdd:COG4988 87 ARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLILLV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 190 TVPI----MFFVTKKLVAYSGKNFAKrqkdLGELNGFIEEAITGadVTTL--YGKEKETVQNFNKINEQLRVSatkadTF 263
Cdd:COG4988 167 TAPLiplfMILVGKGAAKASRRQWRA----LARLSGHFLDRLRG--LTTLklFGRAKAEAERIAEASEDFRKR-----TM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 264 S----AFIfpS---MNFINNLGMGLVIGTGSVMVLNG-MTTVGVIAAFInYSRQFSRPLSQFATLMNTIQAAVAGGERVF 335
Cdd:COG4988 236 KvlrvAFL--SsavLEFFASLSIALVAVYIGFRLLGGsLTLFAALFVLL-LAPEFFLPLRDLGSFYHARANGIAAAEKIF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 336 EIMDEVPEIKNKKDAFVVQNLQGHVALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQG 415
Cdd:COG4988 313 ALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 416 QIHIDGKNIKEYDINSLRGKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGS 495
Cdd:COG4988 393 SILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 496 NLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEK 575
Cdd:COG4988 473 GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQ 552
|
570
....*....|.
gi 1267510758 576 GNHESLMEDRG 586
Cdd:COG4988 553 GTHEELLAKNG 563
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
32-596 |
9.70e-126 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 382.13 E-value: 9.70e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 32 VWNYMGYQKAALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALK 111
Cdd:TIGR02204 9 LWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 112 TIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITV 191
Cdd:TIGR02204 89 VVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 192 PI----MFFVTKKLVAYSGKNfakrQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFI 267
Cdd:TIGR02204 169 PLvllpILLFGRRVRKLSRES----QDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 268 FPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEIMDEVPEIKNK 347
Cdd:TIGR02204 245 TAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 348 KDAFVV-QNLQGHVALENVSFGYEE--NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI 424
Cdd:TIGR02204 325 AHPKTLpVPLRGEIEFEQVNFAYPArpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 425 KEYDINSLRGKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQL 504
Cdd:TIGR02204 405 RQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 505 LAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKGNHESLMED 584
Cdd:TIGR02204 485 IAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAK 564
|
570
....*....|..
gi 1267510758 585 RGFYFDLYTSQF 596
Cdd:TIGR02204 565 GGLYARLARLQF 576
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
107-592 |
3.55e-121 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 369.87 E-value: 3.55e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 107 NVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIV 186
Cdd:COG4987 81 DATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 187 TLITVPIMFFVTKKLVAYSGKNFAKRQKDL-GELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSA 265
Cdd:COG4987 161 LALGLLLAGLLLPLLAARLGRRAGRRLAAArAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 266 FIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFInysrqFSrPLSQFATLMNTIQAAVAGG------ERVFEIMD 339
Cdd:COG4987 241 LAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLV-----LA-ALALFEALAPLPAAAQHLGrvraaaRRLNELLD 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 340 EVPEIKNKKDAfVVQNLQGHVALENVSFGY-EENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIH 418
Cdd:COG4987 315 APPAVTEPAEP-APAPGGPSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSIT 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 419 IDGKNIKEYDINSLRGKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLS 498
Cdd:COG4987 394 LGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLS 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 499 QGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKGNH 578
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTH 553
|
490
....*....|....
gi 1267510758 579 ESLMEDRGFYFDLY 592
Cdd:COG4987 554 EELLAQNGRYRQLY 567
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
358-586 |
1.99e-120 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 355.76 E-value: 1.99e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 358 GHVALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIG 437
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 438 VVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADI 517
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267510758 518 LILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKGNHESLMEDRG 586
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
28-596 |
2.27e-119 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 365.88 E-value: 2.27e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 28 TVMRVWNY-----MGYQKAALTFVIFLVFVTTLLGLLGPYLmgviiDQYIVPKDLSGTARMCLLLIA---IYGVTVF--- 96
Cdd:PRK11176 12 TFRRLWPTiapfkAGLIVAGVALILNAASDTFMLSLLKPLL-----DDGFGKADRSVLKWMPLVVIGlmiLRGITSFiss 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 97 --LTWlqifvmvnVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTI 174
Cdd:PRK11176 87 ycISW--------VSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 175 AMFALDWILAIVTLITVPIMFFVTKkLVAYSGKNFAKR-QKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQL 253
Cdd:PRK11176 159 MMFYYSWQLSLILIVIAPIVSIAIR-VVSKRFRNISKNmQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 254 RVSATKADTFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAafINYSRQFS--RPLSQFATLMNTIQAAVAGG 331
Cdd:PRK11176 238 RQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTIT--VVFSSMIAlmRPLKSLTNVNAQFQRGMAAC 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 332 ERVFEIMDEVPEIKNKKdaFVVQNLQGHVALENVSFGYEENKTI-LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFY 410
Cdd:PRK11176 316 QTLFAILDLEQEKDEGK--RVIERAKGDIEFRNVTFTYPGKEVPaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 411 DIQQGQIHIDGKNIKEYDINSLRGKIGVVLQDTYLFAGTIMDNIRYGRLDA-SDEEVINAAKAASAHSFIKHLPNQYETK 489
Cdd:PRK11176 394 DIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 490 IASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKD 569
Cdd:PRK11176 474 IGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVED 553
|
570 580
....*....|....*....|....*..
gi 1267510758 570 GSIIEKGNHESLMEDRGFYFDLYTSQF 596
Cdd:PRK11176 554 GEIVERGTHAELLAQNGVYAQLHKMQF 580
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
360-592 |
1.13e-118 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 351.53 E-value: 1.13e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKT-ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGV 438
Cdd:cd03251 1 VEFKNVTFRYPGDGPpVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 439 VLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADIL 518
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267510758 519 ILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKGNHESLMEDRGFYFDLY 592
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-591 |
1.29e-116 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 362.50 E-value: 1.29e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 23 KNTKGTVMRVWNYMGYQKAALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTAR----MCLLLIAiYGVTVFLT 98
Cdd:TIGR00958 143 SETADLLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASaiffMCLLSIA-SSVSAGLR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 99 wLQIFvmvNVALKTIQ-KIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMF 177
Cdd:TIGR00958 222 -GGSF---NYTMARINlRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFML 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 178 ALDWILAIVTLITVPIMFFVTKKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFN-KINEQLRVS 256
Cdd:TIGR00958 298 WLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKeALEETLQLN 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 257 ATKADTFSAFIFpSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFE 336
Cdd:TIGR00958 378 KRKALAYAGYLW-TTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 337 IMDEVPEIKNKkDAFVVQNLQGHVALENVSFGY--EENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQ 414
Cdd:TIGR00958 457 YLDRKPNIPLT-GTLAPLNLEGLIEFQDVSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTG 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 415 GQIHIDGKNIKEYDINSLRGKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEG 494
Cdd:TIGR00958 536 GQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKG 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 495 SNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNnlMRGRTSFVIAHRLKTIEKADQILVIKDGSIIE 574
Cdd:TIGR00958 616 SQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVE 693
|
570
....*....|....*..
gi 1267510758 575 KGNHESLMEDRGFYFDL 591
Cdd:TIGR00958 694 MGTHKQLMEDQGCYKHL 710
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
360-595 |
2.07e-110 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 330.35 E-value: 2.07e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVV 439
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILI 519
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267510758 520 LDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKGNHESLMEDRGFYFDLYTSQ 595
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
33-596 |
8.84e-108 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 336.16 E-value: 8.84e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 33 WNYMGYQKAALTFVIFLVFVTTLLGLLG---PYLMGVIIDQyivpkdLSGTARMCLLLIAIYGVTVFltwlQIFVMVNVA 109
Cdd:PRK13657 8 ARVLQYLGAEKRLGILLAVANVLLAAATfaePILFGRIIDA------ISGKGDIFPLLAAWAGFGLF----NIIAGVLVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 110 L-------KTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLnQALTQSVVQIISSALTFIGVTIAM-FALDW 181
Cdd:PRK13657 78 RhadrlahRRRLAVLTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDAL-FGLWLEFMREHLATLVALVVLLPLaLFMNW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 182 ILAIVtLITVPIMFFVTKKLVAysgknfaKRQKDL--------GELNGFIEEAITGADVttlygkeketVQNFNKINEQL 253
Cdd:PRK13657 157 RLSLV-LVVLGIVYTLITTLVM-------RKTKDGqaaveehyHDLFAHVSDAIGNVSV----------VQSYNRIEAET 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 254 RVSATKADTFSAFIFPSMNF------IN----NLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNT 323
Cdd:PRK13657 219 QALRDIADNLLAAQMPVLSWwalasvLNraasTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 324 IQAAVAGGERVFEIMDEVPEIKNKKDAFVVQNLQGHVALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTII 403
Cdd:PRK13657 299 VFMAAPKLEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 404 NLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLP 483
Cdd:PRK13657 379 NLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKP 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 484 NQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQ 563
Cdd:PRK13657 459 DGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADR 538
|
570 580 590
....*....|....*....|....*....|...
gi 1267510758 564 ILVIKDGSIIEKGNHESLMEDRGFYFDLYTSQF 596
Cdd:PRK13657 539 ILVFDNGRVVESGSFDELVARGGRFAALLRAQG 571
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
360-595 |
2.21e-106 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 319.87 E-value: 2.21e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEE--NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIG 437
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 438 VVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADI 517
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 518 LILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKGNHESLMEDRGFYFDLYTSQ 595
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
28-595 |
9.98e-97 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 307.41 E-value: 9.98e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 28 TVMRVWNYMGYQKAALTFVIFLVFVTTLLGLLGPYLMGVIIDQyIVPKD---LSGTARMCLLLIAIYGVTVFLTWLQIFV 104
Cdd:PRK10790 10 TLKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDN-MVAKGnlpLGLVAGLAAAYVGLQLLAAGLHYAQSLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 105 MVNVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQaLTQSVVQIISSALTFIGVT-IAMFALDWIL 183
Cdd:PRK10790 89 FNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRD-LYVTVVATVLRSAALIGAMlVAMFSLDWRM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 184 AIVTLITVPIMFFVTKKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEK---ETVQNFNKINEQLRVSATKA 260
Cdd:PRK10790 168 ALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQArfgERMGEASRSHYMARMQTLRL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 261 DTFsaFIFPSMNFINNL---GMGLVIGTGSVmvlnGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEI 337
Cdd:PRK10790 248 DGF--LLRPLLSLFSALilcGLLMLFGFSAS----GTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 338 MDEvPEIKNKKDAFVVQnlQGHVALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQI 417
Cdd:PRK10790 322 MDG-PRQQYGNDDRPLQ--SGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 418 HIDGKNIKEYDINSLRGKIGVVLQDTYLFAGTIMDNIRYGRlDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNL 497
Cdd:PRK10790 399 RLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 498 SQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKGN 577
Cdd:PRK10790 478 SVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
570
....*....|....*...
gi 1267510758 578 HESLMEDRGFYFDLYTSQ 595
Cdd:PRK10790 558 HQQLLAAQGRYWQMYQLQ 575
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
47-595 |
1.21e-90 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 290.85 E-value: 1.21e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 47 IFLVFVTTLLGLLGPYLMGVIIDQyIVPKDLSgtARMCLLLIAIYGVTVFLTWLQIFV----MVNVALKTIQKIRQDIFE 122
Cdd:PRK10789 1 VALLIIIAMLQLIPPKVVGIIVDG-VTEQHMT--TGQILMWIGTMVLIAVVVYLLRYVwrvlLFGASYQLAVELREDFYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAM-FALDWILAIVTLITVPIMFFVTKKL 201
Cdd:PRK10789 78 QLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMsTQISWQLTLLALLPMPVMAIMIKRY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 202 VAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQ-----LRVSATKAdTFSAFIFPSMNFINN 276
Cdd:PRK10789 158 GDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDtgkknMRVARIDA-RFDPTIYIAIGMANL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 277 LGmglvIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEIMDEVPEIKNKKDAFVVQnl 356
Cdd:PRK10789 237 LA----IGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVPEG-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 357 QGHVALENVSFGYEEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGK 435
Cdd:PRK10789 311 RGELDVNIRQFTYPQTdHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 436 IGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADA 515
Cdd:PRK10789 391 LAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNA 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 516 DILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKGNHESLMEDRGFYFDLYTSQ 595
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
43-334 |
1.40e-87 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 273.49 E-value: 1.40e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 43 LTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVP--KDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDI 120
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPgqGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 121 FEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTKK 200
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 201 LVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMG 280
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1267510758 281 LVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18544 241 LVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
39-567 |
8.27e-87 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 279.56 E-value: 8.27e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 39 QKAALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPK-DLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIR 117
Cdd:TIGR02857 1 ARRALALLALLGVLGALLIIAQAWLLARVVDGLISAGePLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 118 QDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVP-IMFF 196
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPlIPIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 197 VTkkLVAYSGKNFAKRQ-KDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRvSAT----KADTFSAFIfpsM 271
Cdd:TIGR02857 161 MI--LIGWAAQAAARKQwAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYR-ERTmrvlRIAFLSSAV---L 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 272 NFINNLGMGLVIGTGSVMVLNG-MTTVGVIAAFInYSRQFSRPLSQFATLMNTIQAAVAGGERVFEIMDEVPEIK-NKKD 349
Cdd:TIGR02857 235 ELFATLSVALVAVYIGFRLLAGdLDLATGLFVLL-LAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLaGKAP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 350 AFVVQNLQghVALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDI 429
Cdd:TIGR02857 314 VTAAPASS--LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 430 NSLRGKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIAR 509
Cdd:TIGR02857 392 DSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALAR 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 510 AILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVI 567
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
42-334 |
2.07e-85 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 267.80 E-value: 2.07e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 42 ALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDIF 121
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 122 EKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTKKL 201
Cdd:cd18545 81 SHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 202 VAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGL 281
Cdd:cd18545 161 RRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTAL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1267510758 282 VIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18545 241 VYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
28-591 |
3.18e-85 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 277.16 E-value: 3.18e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 28 TVMRVWNYMGYQKAALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTarmcLLLIAIYGVTVFLTwlqiFVMV- 106
Cdd:TIGR01192 6 VYVRALSYLNVHKNRVLLIVIANITLAAITIAEPILFGRIIDAISSKSDVLPT----LALWAGFGVFNTIA----YVLVa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 107 ----NVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWI 182
Cdd:TIGR01192 78 readRLAHGRRATLLTEAFGRIISMPLSWHQQRGTSNALHTLLRATETLFGLWLEFMRQHLATFVALFLLIPTAFAMDWR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 183 LAIVtLITVPIMFFVTKKLVAYSGKNF-AKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKAD 261
Cdd:TIGR01192 158 LSIV-LMVLGILYILIAKLVMQRTKNGqAAVEHHYHNVFKHVSDSISNVSVVHSYNRIEAETSALKQFTNNLLSAQYPVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 262 TFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEIMDEV 341
Cdd:TIGR01192 237 DWWALASGLNRMASTISMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 342 PEIKNKKDAFVVQNLQGHVALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDG 421
Cdd:TIGR01192 317 FQREEPADAPELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 422 KNIKEYDINSLRGKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQ 501
Cdd:TIGR01192 397 IDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 502 KQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKGNHESL 581
Cdd:TIGR01192 477 RQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQEL 556
|
570
....*....|
gi 1267510758 582 MEDRGFYFDL 591
Cdd:TIGR01192 557 IQKDGRFYKL 566
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
360-570 |
2.60e-78 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 244.99 E-value: 2.60e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGV 438
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 439 VLQDTYLFAGTIMDNIrygrldasdeevinaakaasahsfikhlpnqyetkiasegsnLSQGQKQLLAIARAILADADIL 518
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1267510758 519 ILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDG 570
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
43-334 |
5.30e-78 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 248.62 E-value: 5.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 43 LTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDIFE 122
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTKKLV 202
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 203 AYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLV 282
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1267510758 283 IGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
39-593 |
1.13e-77 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 260.06 E-value: 1.13e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 39 QKAALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIvPKDLSGTARMCLL-LIAIYGVTVFLTWLQIFVMV----NVALKTI 113
Cdd:TIGR01193 154 QKKLIVNIVIAAIIVTLISIAGSYYLQKIIDTYI-PHKMMGTLGIISIgLIIAYIIQQILSYIQIFLLNvlgqRLSIDII 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 114 QKIRQDIFEkiqtLSLRFFDVRSQGDLMSRVTnDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPI 193
Cdd:TIGR01193 233 LSYIKHLFE----LPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPV 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 194 MffvtkKLVAYSGKN-FAKRQKDLGE----LNGFIEEAITGADVTTLYGKEKETvqnFNKINEQL------RVSATKADT 262
Cdd:TIGR01193 308 Y-----AVIIILFKRtFNKLNHDAMQanavLNSSIIEDLNGIETIKSLTSEAER---YSKIDSEFgdylnkSFKYQKADQ 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 263 FSAFIFPSMNFINNLgmgLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEIMDEVP 342
Cdd:TIGR01193 380 GQQAIKAVTKLILNV---VILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDS 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 343 EIKNKKDAFVVQNLQGHVALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGK 422
Cdd:TIGR01193 457 EFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 423 NIKEYDINSLRGKIGVVLQDTYLFAGTIMDNIRYG-RLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQ 501
Cdd:TIGR01193 537 SLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQ 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 502 KQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNlMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKGNHESL 581
Cdd:TIGR01193 617 KQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
570
....*....|..
gi 1267510758 582 MEDRGFYFDLYT 593
Cdd:TIGR01193 696 LDRNGFYASLIH 707
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
354-572 |
1.35e-75 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 240.07 E-value: 1.35e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 354 QNLQGHVALENVSFGY--EENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINS 431
Cdd:cd03248 6 DHLKGIVKFQNVTFAYptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 432 LRGKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAI 511
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267510758 512 LADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSI 572
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
360-595 |
9.87e-74 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 235.84 E-value: 9.87e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYE-ENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGV 438
Cdd:cd03252 1 ITFEHVRFRYKpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 439 VLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADIL 518
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267510758 519 ILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKGNHESLMEDRGFYFDLYTSQ 595
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
86-555 |
1.25e-73 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 244.96 E-value: 1.25e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 86 LLIAIYGVTVF------LTWLQIFVMVNVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSV 159
Cdd:TIGR02868 52 LSVAAVAVRAFgigravFRYLERLVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 160 VQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTKKLVAYSGKNFAKRQKDL-GELNGFIEEAITGADVTTLYGK 238
Cdd:TIGR02868 132 VPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAGFVAPLVSLRAARAAEQALARLrGELAAQLTDALDGAAELVASGA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 239 EKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFA 318
Cdd:TIGR02868 212 LPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALP 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 319 TLMNTIQAAVAGGERVFEIMDEVPEIKNKKDAFVVQNLQGHVALE--NVSFGYEENKTILKEVSLKARPGETIALVGPTG 396
Cdd:TIGR02868 292 AAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLElrDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSG 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 397 SGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAH 476
Cdd:TIGR02868 372 SGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLA 451
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267510758 477 SFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRL 555
Cdd:TIGR02868 452 DWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
358-577 |
2.91e-73 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 233.92 E-value: 2.91e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 358 GHVALENVSFGYEEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKI 436
Cdd:cd03244 1 GDIEFKNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 437 GVVLQDTYLFAGTIMDNirygrLD----ASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAIL 512
Cdd:cd03244 81 SIIPQDPVLFSGTIRSN-----LDpfgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267510758 513 ADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKGN 577
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
43-334 |
2.47e-71 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 231.27 E-value: 2.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 43 LTFVIFLVFVTTLLGLLGPYLMGVIIDQ-YIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDIF 121
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLvTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 122 EKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTKKL 201
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 202 VAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGL 281
Cdd:cd18778 161 SKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1267510758 282 VIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18778 241 VLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
111-592 |
2.17e-70 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 237.42 E-value: 2.17e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 111 KTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAI----- 185
Cdd:PRK11160 90 RVLTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADVDTLDHLYLRLISPLVAALVVILVLTIGLSFFDLTLALtlggi 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 186 --VTLITVPIMFFvtkklvaYSGKNFAKRQKDL-GELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKadt 262
Cdd:PRK11160 170 llLLLLLLPLLFY-------RLGKKPGQDLTHLrAQYRVQLTEWLQGQAELTLFGAEDRYRQQLEQTEQQWLAAQRR--- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 263 fsafifpsMNFINNLGMGLVIgtgsvmVLNGMTTVGV--IAAFINYSRQFSRP---LSQFATL-----MNTIQAA----- 327
Cdd:PRK11160 240 --------QANLTGLSQALMI------LANGLTVVLMlwLAAGGVGGNAQPGAliaLFVFAALaafeaLMPVAGAfqhlg 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 328 --VAGGERVFEIMDEVPEIKNKKDAfVVQNLQGHVALENVSFGYEENKT-ILKEVSLKARPGETIALVGPTGSGKTTIIN 404
Cdd:PRK11160 306 qvIASARRINEITEQKPEVTFPTTS-TAAADQVSLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQ 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 405 LLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHsfiKHLPN 484
Cdd:PRK11160 385 LLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLE---KLLED 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 485 Q--YETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKAD 562
Cdd:PRK11160 462 DkgLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFD 541
|
490 500 510
....*....|....*....|....*....|
gi 1267510758 563 QILVIKDGSIIEKGNHESLMEDRGFYFDLY 592
Cdd:PRK11160 542 RICVMDNGQIIEQGTHQELLAQQGRYYQLK 571
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
40-572 |
4.88e-68 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 230.79 E-value: 4.88e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 40 KAALTFVIFLVFVTTLLGLLGP-YLMGViidqYivpkDLSGTAR-------MCLLLIAIYGVTVFLTWLQIFVMVNVALK 111
Cdd:COG4618 19 RRAFLSVGLFSFFINLLMLTPPlYMLQV----Y----DRVLTSRsvdtllmLTLLALGLYAVMGLLDAVRSRILVRVGAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 112 TIQKIRQDIFEKIQTLSLRFFDVRSQGDLmsrvtNDIDNLNQALTqsvvqiiSSALT----------FIGVtiaMFALDW 181
Cdd:COG4618 91 LDRRLGPRVFDAAFRAALRGGGGAAAQAL-----RDLDTLRQFLT-------GPGLFalfdlpwapiFLAV---LFLFHP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 182 ILAIVTLITVPIMF-------FVTKKLVAYSGKNFAKRqkdlgelNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLR 254
Cdd:COG4618 156 LLGLLALVGALVLValallneRLTRKPLKEANEAAIRA-------NAFAEAALRNAEVIEAMGMLPALRRRWQRANARAL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 255 VSATKADTFSAFIfpsMNFINNLGMGL---VIGTGSVMVLNGMTTVGV-IAAFINYSRQFSrPLSQFATLMNTIQAAVAG 330
Cdd:COG4618 229 ALQARASDRAGGF---SALSKFLRLLLqsaVLGLGAYLVIQGEITPGAmIAASILMGRALA-PIEQAIGGWKQFVSARQA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 331 GERVFEIMDEVPEiknKKDAFVVQNLQGHVALENVSFGY-EENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRF 409
Cdd:COG4618 305 YRRLNELLAAVPA---EPERMPLPRPKGRLSVENLTVVPpGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 410 YDIQQGQIHIDGKNIKEYDINSLRGKIGVVLQDTYLFAGTIMDNI-RYGrlDASDEEVINAAKAASAHSFIKHLPNQYET 488
Cdd:COG4618 382 WPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDT 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 489 KIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNL-MRGRTSFVIAHRLKTIEKADQILVI 567
Cdd:COG4618 460 RIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVL 539
|
....*
gi 1267510758 568 KDGSI 572
Cdd:COG4618 540 RDGRV 544
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
358-576 |
1.61e-67 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 218.61 E-value: 1.61e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 358 GHVALENVSFGY--EENKTiLKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGK 435
Cdd:cd03245 1 GRIEFRNVSFSYpnQEIPA-LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 436 IGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADA 515
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267510758 516 DILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKG 576
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
43-334 |
5.45e-67 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 220.07 E-value: 5.45e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 43 LTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARM----CLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQ 118
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGNTSLllllVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 119 DIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVT 198
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 199 KKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLG 278
Cdd:cd18563 161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1267510758 279 MGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18563 241 TLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
43-334 |
7.75e-62 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 206.51 E-value: 7.75e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 43 LTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDIFE 122
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTKKLV 202
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 203 AYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLV 282
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1267510758 283 IGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18542 241 LWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
43-334 |
2.82e-61 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 205.03 E-value: 2.82e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 43 LTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDIFE 122
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTKKLV 202
Cdd:cd18546 81 HLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 203 AYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLV 282
Cdd:cd18546 161 RRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1267510758 283 IGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18546 241 LLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
43-334 |
6.75e-57 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 193.41 E-value: 6.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 43 LTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDIFE 122
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTKKLV 202
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 203 AYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLV 282
Cdd:cd18552 161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1267510758 283 IGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18552 241 LWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
319-593 |
1.65e-55 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 197.76 E-value: 1.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 319 TLMNTIQAAVAGGERVFEImDEVPEIKNKkdAFVVQNLQGHVALENVSFgyeenktilkevSLKArpGETIALVGPTGSG 398
Cdd:PRK11174 326 TFLETPLAHPQQGEKELAS-NDPVTIEAE--DLEILSPDGKTLAGPLNF------------TLPA--GQRIALVGPSGAG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 399 KTTIINLLTRF--YdiqQGQIHIDGKNIKEYDINSLRGKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAH 476
Cdd:PRK11174 389 KTSLLNALLGFlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVS 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 477 SFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLK 556
Cdd:PRK11174 466 EFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLE 545
|
250 260 270
....*....|....*....|....*....|....*..
gi 1267510758 557 TIEKADQILVIKDGSIIEKGNHESLMEDRGFYFDLYT 593
Cdd:PRK11174 546 DLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLA 582
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
43-334 |
2.35e-54 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 186.95 E-value: 2.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 43 LTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLS---------GTARM------CLLLIAIYGVTVFLTWLQIFVMVN 107
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDVLGDKPLPgllglapllGPDPLallllaAAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 108 VALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVT 187
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 188 LITVPIMFFVTKKlvaYSG--KNFAKRQ-KDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFS 264
Cdd:cd18564 161 LAVAPLLLLAARR---FSRriKEASREQrRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQ 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 265 AFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18564 238 ALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
40-334 |
4.95e-54 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 185.76 E-value: 4.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 40 KAALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQD 119
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 120 IFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTk 199
Cdd:cd18540 81 AFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVS- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 200 klvAYSGKNFAKRQKDLGELN----GFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFIN 275
Cdd:cd18540 160 ---IYFQKKILKAYRKVRKINsritGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1267510758 276 NLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18540 237 SIATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
47-334 |
8.59e-54 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 184.92 E-value: 8.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 47 IFLVFVTTLLGLLGPYLMGVIIDQYIVPK-DLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDIFEKIQ 125
Cdd:cd18541 5 ILFLILVDLLQLLIPRIIGRAIDALTAGTlTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 126 TLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTKKLVAYS 205
Cdd:cd18541 85 TLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 206 GKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLVIGT 285
Cdd:cd18541 165 HKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWY 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1267510758 286 GSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18541 245 GGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
33-591 |
3.08e-53 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 196.71 E-value: 3.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 33 WNYMGYQKAALTFVIFLVFVTTLLGLLGP-YLMGVIIDQYIVpkdlSGTARMCLLLIAIYGVTVFLTWLQIFVM-VNVAL 110
Cdd:TIGR00957 956 WDYMKAIGLFITFLSIFLFVCNHVSALASnYWLSLWTDDPMV----NGTQNNTSLRLSVYGALGILQGFAVFGYsMAVSI 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 111 KTIQKIR---QDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVT 187
Cdd:TIGR00957 1032 GGIQASRvlhQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVII 1111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 188 LITVPIMFFVTKKLVAYSGKnfAKRQKDLGE--LNGFIEEAITGADVttlygkeketVQNFNKINEQLRVSATKADTFSA 265
Cdd:TIGR00957 1112 PPLGLLYFFVQRFYVASSRQ--LKRLESVSRspVYSHFNETLLGVSV----------IRAFEEQERFIHQSDLKVDENQK 1179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 266 FIFPSMNFINNLGMGLVIGTGSVMVLNGMTTV--------GVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEI 337
Cdd:TIGR00957 1180 AYYPSIVANRWLAVRLECVGNCIVLFAALFAVisrhslsaGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEY 1259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 338 MdevpeiKNKKDA-FVVQNLQ--------GHVALENVSFGYEEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLT 407
Cdd:TIGR00957 1260 S------ETEKEApWQIQETAppsgwpprGRVEFRNYCLRYREDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLF 1333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 408 RFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVLQDTYLFAGTIMDNIR-YGRLdaSDEEVINAAKAASAHSFIKHLPNQY 486
Cdd:TIGR00957 1334 RINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDpFSQY--SDEEVWWALELAHLKTFVSALPDKL 1411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 487 ETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILV 566
Cdd:TIGR00957 1412 DHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIV 1491
|
570 580
....*....|....*....|....*
gi 1267510758 567 IKDGSIIEKGNHESLMEDRGFYFDL 591
Cdd:TIGR00957 1492 LDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
358-576 |
8.55e-52 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 176.83 E-value: 8.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 358 GHVALENVSFGYEEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKI 436
Cdd:cd03369 5 GEIEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 437 GVVLQDTYLFAGTIMDNI-RYGRLdaSDEEVINAakaasahsfikhlpnqyeTKIASEGSNLSQGQKQLLAIARAILADA 515
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLdPFDEY--SDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267510758 516 DILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKG 576
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
43-334 |
9.06e-51 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 176.86 E-value: 9.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 43 LTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTArmcLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDIFE 122
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGLL---ALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTKKLV 202
Cdd:cd18551 78 RLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 203 AYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLV 282
Cdd:cd18551 158 RRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1267510758 283 IGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18551 238 LGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
43-314 |
8.26e-50 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 173.60 E-value: 8.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 43 LTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLS--GTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDI 120
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPEtqALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 121 FEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTKK 200
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 201 LVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMG 280
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 1267510758 281 LVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPL 314
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
45-334 |
8.71e-50 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 174.12 E-value: 8.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 45 FVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDIFEKI 124
Cdd:cd18548 3 LAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 125 QTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTKKLVAY 204
Cdd:cd18548 83 QSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 205 SGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLVIG 284
Cdd:cd18548 163 AIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILW 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1267510758 285 TGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18548 243 FGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
360-576 |
2.57e-48 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 166.33 E-value: 2.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDiNSLRGKIGV 438
Cdd:cd03247 1 LSINNVSFSYPEQeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 439 VLQDTYLFAGTIMDNIrygrldasdeevinaakaasahsfikhlpnqyetkiaseGSNLSQGQKQLLAIARAILADADIL 518
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 519 ILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKG 576
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
43-334 |
2.59e-48 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 170.36 E-value: 2.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 43 LTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDIFE 122
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTKKLV 202
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 203 AYSGKNFAKRQKDLGELNGFIEE--AITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMG 280
Cdd:cd18550 161 RRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1267510758 281 LVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18550 241 LVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
51-334 |
5.92e-48 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 170.05 E-value: 5.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 51 FVTTLLGLLGPYLMGVIID---------QYIVPKDLSGTARM------CLLLIAIYGVTVFLTWLQIFVMVNVALKTIQK 115
Cdd:cd18565 9 ILNRLFDLAPPLLIGVAIDavfngeasfLPLVPASLGPADPRgqlwllGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 116 IRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMF 195
Cdd:cd18565 89 LRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLII 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 196 FVTKKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFIN 275
Cdd:cd18565 169 AGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVA 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267510758 276 NLGMGLVIGTGSVMVLNGMT------TVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18565 249 GAGFVATFVVGGYWVLDGPPlftgtlTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
43-333 |
1.79e-47 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 168.01 E-value: 1.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 43 LTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDIFE 122
Cdd:cd18549 4 FFLDLFCAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVT---- 198
Cdd:cd18549 84 HLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTiyfn 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 199 KKLVAYSGKNFAKrqkdLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLG 278
Cdd:cd18549 164 KKMKKAFRRVREK----IGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1267510758 279 MGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGER 333
Cdd:cd18549 240 NLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGMAGFER 294
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
360-585 |
2.46e-47 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 165.58 E-value: 2.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVV 439
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQ--DTYLFAGTIMDNIRYG--RLDASDEEVINAAKAASAHSFIKHLPNQyetkiasEGSNLSQGQKQLLAIARAILADA 515
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVAFGpeNLGLPREEIRERVEEALELVGLEHLADR-------PPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267510758 516 DILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIA-HRLKTIEK-ADQILVIKDGSIIEKGNHESLMEDR 585
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
46-595 |
1.90e-46 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 176.37 E-value: 1.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 46 VIFLVFV-TTLLGLLGPYLM---GVIIDQYIVPKDLSGTArMCLLLIAIygVTVFLTWLQIFVMVNVALKTIQKIRQDIF 121
Cdd:PTZ00265 61 LLGVSFVcATISGGTLPFFVsvfGVIMKNMNLGENVNDII-FSLVLIGI--FQFILSFISSFCMDVVTTKILKTLKLEFL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 122 EKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVtkKL 201
Cdd:PTZ00265 138 KSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYIC--GV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 202 VAYSGKNFAKRQKDLGELN--GFIEEAITGADVTTLYGKEKETVQNFNkINEQLrvsatkadtFSAFIFPSmNFINNLGM 279
Cdd:PTZ00265 216 ICNKKVKINKKTSLLYNNNtmSIIEEALVGIRTVVSYCGEKTILKKFN-LSEKL---------YSKYILKA-NFMESLHI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 280 GLVIG-----------TGSVMVLN------------GMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAvaggERVFE 336
Cdd:PTZ00265 285 GMINGfilasyafgfwYGTRIIISdlsnqqpnndfhGGSVISILLGVLISMFMLTIILPNITEYMKSLEAT----NSLYE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 337 IMDEVPEIKNKKDAFVVQNLQgHVALENVSFGYEENK--TILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQ 414
Cdd:PTZ00265 361 IINRKPLVENNDDGKKLKDIK-KIQFKNVRFHYDTRKdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 415 GQIHI-DGKNIKEYDINSLRGKIGVVLQDTYLFAGTIMDNIRYG-----RLDA--------------------------- 461
Cdd:PTZ00265 440 GDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkDLEAlsnyynedgndsqenknkrnscrakca 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 462 -------------------------SDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADAD 516
Cdd:PTZ00265 520 gdlndmsnttdsneliemrknyqtiKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPK 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 517 ILILDEATSNIDTRTELQIQEGLNNLM--RGRTSFVIAHRLKTIEKADQILVIKD------------------------- 569
Cdd:PTZ00265 600 ILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSNrergstvdvdiigedptkdnkennn 679
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1267510758 570 ---------------------GS-IIEKGNHESLMEDR-GFYFDLYTSQ 595
Cdd:PTZ00265 680 knnkddnnnnnnnnnnkinnaGSyIIEQGTHDALMKNKnGIYYTMINNQ 728
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
47-334 |
2.91e-46 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 164.58 E-value: 2.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 47 IFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDIFEKIQT 126
Cdd:cd18576 2 LILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 127 LSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTKklvaYSG 206
Cdd:cd18576 82 LPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAV----LFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 207 KNF----AKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLV 282
Cdd:cd18576 158 RRIrklsKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1267510758 283 IGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18576 238 LWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
42-334 |
1.42e-45 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 162.65 E-value: 1.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 42 ALTFVifLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDIF 121
Cdd:cd18543 2 ILALL--AALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 122 EKIQTLSLRFFD-VRSqGDLMSRVTNDIdNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTkk 200
Cdd:cd18543 80 AHLQRLDGAFHDrWQS-GQLLSRATSDL-SLVQRFLAFGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVA-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 201 lVAYSGKNFA---KRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNL 277
Cdd:cd18543 156 -RRFRRRYFPasrRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPEL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1267510758 278 GMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18543 235 GLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
362-572 |
6.97e-44 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 154.30 E-value: 6.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEENKT-ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVL 440
Cdd:cd03246 3 VENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 441 QDTYLFAGTIMDNIrygrldasdeevinaakaasahsfikhlpnqyetkiasegsnLSQGQKQLLAIARAILADADILIL 520
Cdd:cd03246 83 QDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1267510758 521 DEATSNIDTRTELQIQEGLNNL-MRGRTSFVIAHRLKTIEKADQILVIKDGSI 572
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
107-582 |
2.72e-43 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 167.13 E-value: 2.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 107 NVALKTIQK-IRQDIFEKIQTLSLRFFDVRSQ--GDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWIL 183
Cdd:PTZ00265 891 NVIGEKVEKtMKRRLFENILYQEISFFDQDKHapGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 184 AIVTLITVPIMFFV-------------TKKLVAYSGKNFAKRQKD--LGELNGFIEEAITGADVTTLYGKEK------ET 242
Cdd:PTZ00265 971 AAVLTGTYFIFMRVfairarltankdvEKKEINQPGTVFAYNSDDeiFKDPSFLIQEAFYNMNTVIIYGLEDyfcnliEK 1050
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 243 VQNFNKINEQLRVSATKAdtFSAFIFPSMNFINNLGM---GLVIGTGSVMVLNGMTTVGVIAAFINYSrqfsrplSQFAT 319
Cdd:PTZ00265 1051 AIDYSNKGQKRKTLVNSM--LWGFSQSAQLFINSFAYwfgSFLIRRGTILVDDFMKSLFTFLFTGSYA-------GKLMS 1121
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 320 LMNTIQAAVAGGERVFEIMDEVPEIKNKKDAFV-VQN---LQGHVALENVSFGY--EENKTILKEVSLKARPGETIALVG 393
Cdd:PTZ00265 1122 LKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIrIKNkndIKGKIEIMDVNFRYisRPNVPIYKDLTFSCDSKKTTAIVG 1201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 394 PTGSGKTTIINLLTRFYDIQQ------------------------------------------------------GQIHI 419
Cdd:PTZ00265 1202 ETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknsGKILL 1281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 420 DGKNIKEYDINSLRGKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQ 499
Cdd:PTZ00265 1282 DGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSG 1361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 500 GQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNL--MRGRTSFVIAHRLKTIEKADQILVI----KDGSII 573
Cdd:PTZ00265 1362 GQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFV 1441
|
570
....*....|
gi 1267510758 574 E-KGNHESLM 582
Cdd:PTZ00265 1442 QaHGTHEELL 1451
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
362-570 |
5.46e-43 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 153.01 E-value: 5.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEE-NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVL 440
Cdd:cd03225 2 LKNLSFSYPDgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 441 Q--DTYLFAGTIMDNIRYG--RLDASDEEVINAAKAASAHSFIKHLPNQyetkiasEGSNLSQGQKQLLAIARAILADAD 516
Cdd:cd03225 82 QnpDDQFFGPTVEEEVAFGleNLGLPEEEIEERVEEALELVGLEGLRDR-------SPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1267510758 517 ILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIA-HRLKTI-EKADQILVIKDG 570
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLlELADRVIVLEDG 210
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
47-334 |
2.97e-42 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 153.87 E-value: 2.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 47 IFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDIFEKIQT 126
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 127 LSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTKKLVAYSG 206
Cdd:cd18557 82 QEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 207 KNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLVIGTG 286
Cdd:cd18557 162 KLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1267510758 287 SVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18557 242 GYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
360-576 |
2.01e-41 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 149.64 E-value: 2.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQ-----GQIHIDGKNIKE--YDINSL 432
Cdd:cd03260 1 IELRDLNVYYGD-KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDldVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 433 RGKIGVVLQDTYLFAGTIMDNIRYG-RL------DASDEEVINAAKAAsahsfikHLPNqyETKIASEGSNLSQGQKQLL 505
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlRLhgiklkEELDERVEEALRKA-------ALWD--EVKDRLHALGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267510758 506 AIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKG 576
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFG 222
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
356-582 |
4.92e-41 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 149.29 E-value: 4.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 356 LQGHVALENVSFGYEEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRG 434
Cdd:cd03288 16 LGGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 435 KIGVVLQDTYLFAGTIMDNIRYGRlDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILAD 514
Cdd:cd03288 96 RLSIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 515 ADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKGNHESLM 582
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
376-525 |
1.12e-40 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 144.71 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVLQDTYLFAG-TIMDNI 454
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267510758 455 RYGRLdasDEEVINAAKAASAHSFIKHL--PNQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATS 525
Cdd:pfam00005 81 RLGLL---LKGLSKREKDARAEEALEKLglGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
119-585 |
6.13e-40 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 156.86 E-value: 6.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 119 DIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISsalTFIGVTIAMFALDWILAIVTLITVPIMFFVT 198
Cdd:PTZ00243 1036 DLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQ---CLFSICSSILVTSASQPFVLVALVPCGYLYY 1112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 199 KKLVAYSGKNFA-KRQKDLGE--LNGFIEEAITGADVTTLYGKEKETVQnfnkinEQLRvsatKAD-TFSAFIFPSM--- 271
Cdd:PTZ00243 1113 RLMQFYNSANREiRRIKSVAKspVFTLLEEALQGSATITAYGKAHLVMQ------EALR----RLDvVYSCSYLENVanr 1182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 272 ------NFINNLGMGLV--IGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEIMDEV-- 341
Cdd:PTZ00243 1183 wlgvrvEFLSNIVVTVIalIGVIGTMLRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDEVph 1262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 342 ---PEIKNKKDAF-------------VV-----------QNLQ-GHVALENVSFGYEEN-KTILKEVSLKARPGETIALV 392
Cdd:PTZ00243 1263 edmPELDEEVDALerrtgmaadvtgtVViepasptsaapHPVQaGSLVFEGVQMRYREGlPLVLRGVSFRIAPREKVGIV 1342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 393 GPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVLQDTYLFAGTIMDNIRyGRLDASDEEVINAAKA 472
Cdd:PTZ00243 1343 GRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALEL 1421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 473 ASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILIL-DEATSNIDTRTELQIQEGLNNLMRGRTSFVI 551
Cdd:PTZ00243 1422 VGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITI 1501
|
490 500 510
....*....|....*....|....*....|....
gi 1267510758 552 AHRLKTIEKADQILVIKDGSIIEKGNHESLMEDR 585
Cdd:PTZ00243 1502 AHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
362-586 |
2.27e-39 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 144.23 E-value: 2.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDiNSLRGKIGVVLQ 441
Cdd:COG4555 4 VENLSKKYG-KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 442 DTYLFAG-TIMDNIRY-GRLDASDEEVINAAKAASAHSFIkhLPNQYETKIasegSNLSQGQKQLLAIARAILADADILI 519
Cdd:COG4555 82 ERGLYDRlTVRENIRYfAELYGLFDEELKKRIEELIELLG--LEEFLDRRV----GELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267510758 520 LDEATSNIDTRTELQIQEGLNNLMRGRTSFVIA-HRLKTIEK-ADQILVIKDGSIIEKGNHESLMEDRG 586
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-589 |
1.17e-38 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 152.82 E-value: 1.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 33 WN-YMGYQKAA----LTFVIFLVFVTT-LLGLLGPYLMGVIIDQYiVPKDLSGTarmclLLIAIYGVTVF----LTWLQI 102
Cdd:PLN03232 898 WNvLMRYNKAVgglwVVMILLVCYLTTeVLRVSSSTWLSIWTDQS-TPKSYSPG-----FYIVVYALLGFgqvaVTFTNS 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 103 FVMVNVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQaltqSVVQIISSALTFIGVTIAMFALDWI 182
Cdd:PLN03232 972 FWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDR----NVANLMNMFMNQLWQLLSTFALIGT 1047
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 183 LAIVTLITV-PIMFFVTKKLVAYSGKNFAKRQKDlgelngfieeAITGADVTTLYGKEK---ETVQNFNKINEQLRVSAT 258
Cdd:PLN03232 1048 VSTISLWAImPLLILFYAAYLYYQSTSREVRRLD----------SVTRSPIYAQFGEALnglSSIRAYKAYDRMAKINGK 1117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 259 KADTFSAFIFPSMNF-------INNLGMGLVIGTGSVMVL-NGMT--------TVGVIAAF-INYSRQFSRPLSQFATLM 321
Cdd:PLN03232 1118 SMDNNIRFTLANTSSnrwltirLETLGGVMIWLTATFAVLrNGNAenqagfasTMGLLLSYtLNITTLLSGVLRQASKAE 1197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 322 NTIQAAvaggERVFEIMD---EVPEIKNKKDAFVVQNLQGHVALENVSFGYE-ENKTILKEVSLKARPGETIALVGPTGS 397
Cdd:PLN03232 1198 NSLNSV----ERVGNYIDlpsEATAIIENNRPVSGWPSRGSIKFEDVHLRYRpGLPPVLHGLSFFVSPSEKVGVVGRTGA 1273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 398 GKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVLQDTYLFAGTIMDNIRYGRlDASDEEVINAAKAASAHS 477
Cdd:PLN03232 1274 GKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFS-EHNDADLWEALERAHIKD 1352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 478 FIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKT 557
Cdd:PLN03232 1353 VIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNT 1432
|
570 580 590
....*....|....*....|....*....|..
gi 1267510758 558 IEKADQILVIKDGSIIEKGNHESLMEDRGFYF 589
Cdd:PLN03232 1433 IIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
40-334 |
1.98e-38 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 143.36 E-value: 1.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 40 KAALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQD 119
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 120 IFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTK 199
Cdd:cd18570 81 YFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 200 KLVaysgKNFAKRQKDL----GELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFIN 275
Cdd:cd18570 160 LFN----KPFKKKNREVmesnAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLIS 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1267510758 276 NLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18570 236 LIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
360-582 |
2.10e-37 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 139.41 E-value: 2.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVV 439
Cdd:COG1120 2 LEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQDTYL-FAGTIMDNIRYGR---------LDASDEEVINAAKAASAhsfIKHLPNQYETkiasegsNLSQGQKQLLAIAR 509
Cdd:COG1120 81 PQEPPApFGLTVRELVALGRyphlglfgrPSAEDREAVEEALERTG---LEHLADRPVD-------ELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 510 AILADADILILDEATSNIDTRTELQIQEGLNNL--MRGRTSFVIAH------RLktiekADQILVIKDGSIIEKGNHESL 581
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHdlnlaaRY-----ADRLVLLKDGRIVAQGPPEEV 225
|
.
gi 1267510758 582 M 582
Cdd:COG1120 226 L 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
360-584 |
2.88e-37 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 145.05 E-value: 2.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENK----TILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI---KEYDINSL 432
Cdd:COG1123 261 LEVRNLSKRYPVRGkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLtklSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 433 RGKIGVVLQDTY--LFAG-TIMDNIRYG---RLDASDEEVinAAKAASA-------HSFIKHLPNQyetkiasegsnLSQ 499
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRmTVGDIIAEPlrlHGLLSRAER--RERVAELlervglpPDLADRYPHE-----------LSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 500 GQKQLLAIARAILADADILILDEATSNIDTRTELQIqegLNNLMR-----GRTSFVIAHRLKTIEK-ADQILVIKDGSII 573
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQI---LNLLRDlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRIV 484
|
250
....*....|.
gi 1267510758 574 EKGNHESLMED 584
Cdd:COG1123 485 EDGPTEEVFAN 495
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
362-570 |
6.26e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 134.68 E-value: 6.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVLQ 441
Cdd:cd00267 2 IENLSFRYGG-RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 442 dtylfagtimdnirygrldasdeevinaakaasahsfikhlpnqyetkiasegsnLSQGQKQLLAIARAILADADILILD 521
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1267510758 522 EATSNIDTRTELQIQEGLNNLM-RGRTSFVIAHRLKTIEKA-DQILVIKDG 570
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
360-572 |
2.41e-36 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 133.68 E-value: 2.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEyDINSLRGKIGVV 439
Cdd:cd03230 1 IEVRNLSKRYG-KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQDTYLFAG-TIMDNIRYgrldasdeevinaakaasahsfikhlpnqyetkiasegsnlSQGQKQLLAIARAILADADIL 518
Cdd:cd03230 79 PEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1267510758 519 ILDEATSNIDTRTELQIQEGLNNLM-RGRTSFVIAHRLKTIEK-ADQILVIKDGSI 572
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
360-574 |
4.37e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 134.79 E-value: 4.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGY---EENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSL---- 432
Cdd:COG1136 5 LELRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 433 RGKIGVVLQDTYLFAG-TIMDNI----RYGRLDASDEEvinaAKAASA------HSFIKHLPNQyetkiasegsnLSQGQ 501
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENValplLLAGVSRKERR----ERARELlervglGDRLDHRPSQ-----------LSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267510758 502 KQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTIEKADQILVIKDGSIIE 574
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
358-589 |
4.39e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 145.27 E-value: 4.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 358 GHVALENVSFGYEEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKI 436
Cdd:PLN03130 1236 GSIKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 437 GVVLQDTYLFAGTIMDNirygrLDA----SDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAIL 512
Cdd:PLN03130 1316 GIIPQAPVLFSGTVRFN-----LDPfnehNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267510758 513 ADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKGNHESLMEDRGFYF 589
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAF 1467
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
360-571 |
6.49e-36 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 133.36 E-value: 6.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKT----ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIdgknikeydinslRGK 435
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-------------PGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 436 IGVVLQDTYLFAGTIMDNIRYGR-LDASD-EEVInaaKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILA 513
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKpFDEERyEKVI---KACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 514 DADILILDEATSNIDTRTELQIQEG--LNNLMRGRTSFVIAHRLKTIEKADQILVIKDGS 571
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
360-584 |
3.14e-35 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 139.27 E-value: 3.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEEN-KTILKEVSLKARPGETIALVGPTGSGKTTI---INLLTRFYDIQQGQIHIDGKNIKEYDINSLRGK 435
Cdd:COG1123 5 LEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLalaLMGLLPHGGRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 436 IGVVLQD--TYLFAGTIMDNIRYG--RLDASDEEVINAAKAASAHSFIKHLPNQYEtkiasegSNLSQGQKQLLAIARAI 511
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGLERRLDRYP-------HQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267510758 512 LADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTI-EKADQILVIKDGSIIEKGNHESLMED 584
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
362-576 |
3.63e-35 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 132.24 E-value: 3.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEENK---TILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYD--INSLRGK- 435
Cdd:cd03257 4 VKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrLRKIRRKe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 436 IGVVLQDTY-----LFagTIMDNIrygrldasdEEVINAAKAASAHSFIK----------HLPNQYETKIASEgsnLSQG 500
Cdd:cd03257 84 IQMVFQDPMsslnpRM--TIGEQI---------AEPLRIHGKLSKKEARKeavllllvgvGLPEEVLNRYPHE---LSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267510758 501 QKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNL--MRGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKG 576
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqeELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
360-574 |
7.42e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 131.33 E-value: 7.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKN---IKEYDINSLRGKI 436
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 437 GVVLQDTYLFAG-TIMDNIRY-----GRLDASDEEVINAA--------KAasahsfiKHLPNQyetkiasegsnLSQGQK 502
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENVALplrvtGKSRKEIRRRVREVldlvglsdKA-------KALPHE-----------LSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267510758 503 QLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIA-HRLKTIEKADQ-ILVIKDGSIIE 574
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
360-574 |
1.57e-34 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 131.08 E-value: 1.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGY---EENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKI 436
Cdd:COG1124 2 LEVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 437 GVVLQDTYL-------FAGTIMDNIRYGRLDASDEEVINAAKAAS-AHSFIKHLPNQyetkiasegsnLSQGQKQLLAIA 508
Cdd:COG1124 82 QMVFQDPYAslhprhtVDRILAEPLRIHGLPDREERIAELLEQVGlPPSFLDRYPHQ-----------LSGGQRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267510758 509 RAILADADILILDEATSNIDTRTELQIQEGLNNLM--RGRTSFVIAHRLKTIEK-ADQILVIKDGSIIE 574
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLReeRGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVE 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
362-570 |
1.66e-33 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 126.15 E-value: 1.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINS--LRGKIGVV 439
Cdd:cd03229 3 LKNVSKRYGQ-KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQDTYLFAG-TIMDNIRYGrldasdeevinaakaasahsfikhlpnqyetkiasegsnLSQGQKQLLAIARAILADADIL 518
Cdd:cd03229 82 FQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1267510758 519 ILDEATSNIDTRTELQIQEGLNNL--MRGRTSFVIAHRLKTIEK-ADQILVIKDG 570
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
360-582 |
4.42e-33 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 127.03 E-value: 4.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVV 439
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQDTYLFAG-TIMDNIR-YGRLDASDEEVInAAKAASAHSFIKHLPNQYETKIASEgsnLSQGQKQLLAIARAILADADI 517
Cdd:cd03295 81 IQQIGLFPHmTVEENIAlVPKLLKWPKEKI-RERADELLALVGLDPAEFADRYPHE---LSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 518 LILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRL-KTIEKADQILVIKDGSIIEKGNHESLM 582
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
360-572 |
8.98e-33 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 125.29 E-value: 8.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKT---ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSL---- 432
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 433 RGKIGVVLQDTYLFAG-TIMDNIRY-----GRLDASDEEVINAA--KAASAHSfIKHLPNQyetkiasegsnLSQGQKQL 504
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELplllaGVPKKERRERAEELleRVGLGDR-LNHYPSE-----------LSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 505 LAIARAILADADILILDEATSNIDTRTELQIQEGLNNL--MRGRTSFVIAHRLKTIEKADQILVIKDGSI 572
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
360-574 |
9.78e-33 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 125.28 E-value: 9.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEEN---KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeyDINSLRGKI 436
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 437 GVVLQDTYLFA-GTIMDNIRYG----RLDASD--EEVINAAKAASAHSFIKHLPNQyetkiasegsnLSQGQKQLLAIAR 509
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelqGVPKAEarERAEELLELVGLSGFENAYPHQ-----------LSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267510758 510 AILADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHrlkTIEKA----DQILVI--KDGSIIE 574
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTH---DIDEAvflaDRVVVLsaRPGRIVA 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
361-576 |
1.21e-32 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 123.70 E-value: 1.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 361 ALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVL 440
Cdd:cd03214 1 EVENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 441 QdtylfagtIMDnirygRLDASDEevinaakaasAHSFIkhlpnqyetkiasegSNLSQGQKQLLAIARAILADADILIL 520
Cdd:cd03214 80 Q--------ALE-----LLGLAHL----------ADRPF---------------NELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1267510758 521 DEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLK-TIEKADQILVIKDGSIIEKG 576
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
362-576 |
4.40e-32 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 123.01 E-value: 4.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINslRGKIGVVLQ 441
Cdd:cd03259 3 LKGLSKTYGS-VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 442 DTYLFAG-TIMDNIRYG-RLDASDEEVINAAKAASA-----HSFIKHLPNQyetkiasegsnLSQGQKQLLAIARAILAD 514
Cdd:cd03259 80 DYALFPHlTVAENIAFGlKLRGVPKAEIRARVRELLelvglEGLLNRYPHE-----------LSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267510758 515 ADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRL-KTIEKADQILVIKDGSIIEKG 576
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQeEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
362-573 |
5.90e-32 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 122.75 E-value: 5.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDinsLRGKIGVVLQ 441
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 442 DT--YLFAGTIMDNIRYGRLDASD-----EEV---INAAKAASAHSFIkhlpnqyetkiasegsnLSQGQKQLLAIARAI 511
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAgneqaETVlkdLDLYALKERHPLS-----------------LSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267510758 512 LADADILILDEATSNIDTRTELQIQEGLNNLM-RGRTSFVIAHRLKTIEK-ADQILVIKDGSII 573
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
360-572 |
7.43e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 123.66 E-value: 7.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEydinsLRGKIGVV 439
Cdd:COG1121 7 IELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQDTYL---FAGTIMDNI---RYG------RLDASDEEVINAA-KAASAHSFIKHlpnqyetKIasegSNLSQGQKQLLA 506
Cdd:COG1121 81 PQRAEVdwdFPITVRDVVlmgRYGrrglfrRPSRADREAVDEAlERVGLEDLADR-------PI----GELSGGQQQRVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 507 IARAILADADILILDEATSNIDTRTELQIQEGLNNL-MRGRTSFVIAHRLKTIEK-ADQILVIKDGSI 572
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
358-588 |
5.06e-31 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 122.27 E-value: 5.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 358 GHVALENVSFGY-EENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQqGQIHIDGKNIKEYDINSLRGKI 436
Cdd:cd03289 1 GQMTVKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 437 GVVLQDTYLFAGTIMDNIR-YGRLdaSDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADA 515
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267510758 516 DILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKGNHESLMEDRGFY 588
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
47-334 |
7.32e-31 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 121.88 E-value: 7.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 47 IFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDIFEKIQT 126
Cdd:cd18572 2 FVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 127 LSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTKKLVAYSG 206
Cdd:cd18572 82 QDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 207 KNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLVIGTG 286
Cdd:cd18572 162 KLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1267510758 287 SVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18572 242 GHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
360-583 |
7.70e-31 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 120.47 E-value: 7.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI---KEYDINSLRGKI 436
Cdd:COG1127 6 IEVRNLTKSFGD-RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 437 GVVLQDTYLFAG-TIMDNI-----RYGRLDAS--DEEVINAAKAASAHSFIKHLPNQyetkiasegsnLSQGQKQLLAIA 508
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVafplrEHTDLSEAeiRELVLEKLELVGLPGAADKMPSE-----------LSGGMRKRVALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 509 RAILADADILILDEATSNIDTRTELQIqeglNNLMR------GRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESL 581
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVI----DELIRelrdelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
..
gi 1267510758 582 ME 583
Cdd:COG1127 230 LA 231
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
362-568 |
1.74e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 118.79 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEydinsLRGKIGVVLQ 441
Cdd:cd03235 2 VEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 442 DTYL---FAGTIMDNI---RYG------RLDASDEEVINAAKAASAhsfIKHLPNQyetKIasegSNLSQGQKQLLAIAR 509
Cdd:cd03235 76 RRSIdrdFPISVRDVVlmgLYGhkglfrRLSKADKAKVDEALERVG---LSELADR---QI----GELSGGQQQRVLLAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267510758 510 AILADADILILDEATSNIDTRTELQIQEGLNNL-MRGRTSFVIAHRLKTIEK-ADQILVIK 568
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLLN 206
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
41-334 |
2.44e-30 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 120.66 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 41 AALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIvpkdLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDI 120
Cdd:cd18577 11 AGAALPLMTIVFGDLFDAFTDFGSGESSPDEF----LDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 121 FEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFI-GVTIAmFALDWILAIVTLITVPIMFFVTK 199
Cdd:cd18577 87 LKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIaGFIIA-FIYSWKLTLVLLATLPLIAIVGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 200 KLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGM 279
Cdd:cd18577 166 IMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMY 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267510758 280 GLVIGTGSVMVLNGMTTVG-VIAAFIN-----YSrqfsrpLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18577 246 ALAFWYGSRLVRDGEISPGdVLTVFFAvligaFS------LGQIAPNLQAFAKARAAAAKI 300
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
362-587 |
3.03e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 119.71 E-value: 3.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEENKT-ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVL 440
Cdd:PRK13632 10 VENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 441 Q--DTYLFAGTIMDNIRYG----RLDASDEEVI--NAAKAASAHSFIKHLPnqyetkiasegSNLSQGQKQLLAIARAIL 512
Cdd:PRK13632 90 QnpDNQFIGATVEDDIAFGlenkKVPPKKMKDIidDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267510758 513 ADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIA--HRLKTIEKADQILVIKDGSIIEKGNHESLMEDRGF 587
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEI 235
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
362-576 |
4.15e-30 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 118.37 E-value: 4.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI---KEYDINSLRGKIGV 438
Cdd:cd03261 3 LRGLTKSFGG-RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRLRRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 439 VLQDTYLFAG-TIMDNI-----RYGRLDAS--DEEVINAAKAASAHSFIKHLPnqyetkiasegSNLSQGQKQLLAIARA 510
Cdd:cd03261 82 LFQSGALFDSlTVFENVafplrEHTRLSEEeiREIVLEKLEAVGLRGAEDLYP-----------AELSGGMKKRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267510758 511 ILADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKG 576
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEG 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
359-574 |
1.05e-29 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 117.88 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 359 HVALENVSFGYEENK---TILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEydinsLRGK 435
Cdd:COG1116 7 ALELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 436 IGVVLQDTYLFA-GTIMDNIRYGrLDASDEEVINAAKAASAH-------SFIKHLPNQyetkiasegsnLSQGQKQLLAI 507
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALG-LELRGVPKAERRERARELlelvglaGFEDAYPHQ-----------LSGGMRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267510758 508 ARAILADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAH------RLktiekADQILVIKD--GSIIE 574
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
47-334 |
2.51e-29 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 117.91 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 47 IFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIyGVTVFltwlqIFVMVNV-------------ALKTI 113
Cdd:cd18554 5 IVIGLVRFGIPLLLPLILKYIVDDVIQGSSLTLDEKVYKLFTII-GIMFF-----IFLILRPpveyyrqyfaqwiANKIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 114 QKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPI 193
Cdd:cd18554 79 YDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 194 MFFvtkkLVAYSGKNFAK----RQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFP 269
Cdd:cd18554 159 YIL----AVKYFFGRLRKltkeRSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFS 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267510758 270 SMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18554 235 AVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
362-585 |
7.24e-29 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 114.97 E-value: 7.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI---KEYDINSLRGKIGV 438
Cdd:cd03256 3 VENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 439 VLQDTYLFAG-TIMDNIRYGRLdasdeevinaakaaSAHSFIKHLPNQY---ETKIASE--------------GSNLSQG 500
Cdd:cd03256 83 IFQQFNLIERlSVLENVLSGRL--------------GRRSTWRSLFGLFpkeEKQRALAalervglldkayqrADQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 501 QKQLLAIARAILADADILILDEATSNIDTRTELQIQEGL--NNLMRGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGN 577
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkrINREEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGP 228
|
....*...
gi 1267510758 578 HESLMEDR 585
Cdd:cd03256 229 PAELTDEV 236
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
43-588 |
1.17e-28 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 122.33 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 43 LTFVIFLVFVTTllGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYgVTVFLTWLQIFVMVNVA------------- 109
Cdd:TIGR01271 872 FCLVIFLAEVAA--SLLGLWLITDNPSAPNYVDQQHANASSPDVQKPVI-ITPTSAYYIFYIYVGTAdsvlalgffrglp 948
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 110 -LKTIQKIRQDIFEKIQTLSLR----FFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGvTIAMFALDWILA 184
Cdd:TIGR01271 949 lVHTLLTVSKRLHEQMLHSVLQapmaVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLG-AIFVVSVLQPYI 1027
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 185 IVTLITVPIMFFVtkkLVAYsgknFAKRQKDLGELNGFIEEAITGADVTTL--------YGKEKETVQNFNK-IN----- 250
Cdd:TIGR01271 1028 FIAAIPVAVIFIM---LRAY----FLRTSQQLKQLESEARSPIFSHLITSLkglwtiraFGRQSYFETLFHKaLNlhtan 1100
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 251 -----EQLRVSATKADTFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSrplsqfaTLMNTIq 325
Cdd:TIGR01271 1101 wflylSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVD-------GLMRSV- 1172
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 326 aavaggERVFEIMD---EVPEIKNK------KDAFVVQNL--------QGHVALENVSFGY-EENKTILKEVSLKARPGE 387
Cdd:TIGR01271 1173 ------SRVFKFIDlpqEEPRPSGGggkyqlSTVLVIENPhaqkcwpsGGQMDVQGLTAKYtEAGRAVLQDLSFSVEGGQ 1246
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 388 TIALVGPTGSGKTTIINLLTRFYDiQQGQIHIDGKNIKEYDINSLRGKIGVVLQDTYLFAGTIMDNIR-YGRLdaSDEEV 466
Cdd:TIGR01271 1247 RVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDpYEQW--SDEEI 1323
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 467 INAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGR 546
Cdd:TIGR01271 1324 WKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNC 1403
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1267510758 547 TSFVIAHRLKTIEKADQILVIKDGSIIEKGNHESLMEDRGFY 588
Cdd:TIGR01271 1404 TVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
360-576 |
1.45e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 115.11 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKTI-LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGV 438
Cdd:PRK13635 6 IRVEHISFRYPDAATYaLKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 439 VLQ--DTYLFAGTIMDNIRYG-------RlDASDEEVINAAKAASAHSFIKHLPnqyetkiasegSNLSQGQKQLLAIAR 509
Cdd:PRK13635 86 VFQnpDNQFVGATVQDDVAFGlenigvpR-EEMVERVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267510758 510 AILADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTIEKADQILVIKDGSIIEKG 576
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqkGITVLSITHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
360-581 |
2.32e-28 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 113.44 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENK---TILKEVSLKARPGETIALVGPTGSGKTT---IINLLTRfYDiqQGQIHIDGKNIKEYDINSLR 433
Cdd:cd03258 2 IELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLER-PT--SGSVLVDGTDLTLLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 434 G---KIGVVLQDTYLFAG-TIMDNIRYG-RLDASDEEVINAAkaasahsfIKHLPNQ--YETKIASEGSNLSQGQKQLLA 506
Cdd:cd03258 79 KarrRIGMIFQHFNLLSSrTVFENVALPlEIAGVPKAEIEER--------VLELLELvgLEDKADAYPAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 507 IARAILADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESL 581
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
360-584 |
3.22e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 114.06 E-value: 3.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVV 439
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQ--DTYLFAGTIMDNIRYG----RLDASD-EEVINAAKAASAHSFIKHLPNQYetkiasegsnLSQGQKQLLAIARAIL 512
Cdd:PRK13647 85 FQdpDDQVFSSTVWDDVAFGpvnmGLDKDEvERRVEEALKAVRMWDFRDKPPYH----------LSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267510758 513 ADADILILDEATSNIDTR---TELQIQEGLNNlmRGRTSFVIAHRLK-TIEKADQILVIKDGSIIEKGNHESLMED 584
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRgqeTLMEILDRLHN--QGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
364-572 |
8.06e-28 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 111.08 E-value: 8.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 364 NVSFGyeeNKTILKEVSLKARPGETIALVGPTGSGKTTI---INLLTRfydIQQGQIHIDGKNI--KEYDINSLRGKIGV 438
Cdd:cd03262 7 HKSFG---DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTIIIDGLKLtdDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 439 VLQDTYLFAG-TIMDNIRYG---RLDASDEEVINAAKAASAHSFIKHLPNQYEtkiasegSNLSQGQKQLLAIARAILAD 514
Cdd:cd03262 81 VFQQFNLFPHlTVLENITLApikVKGMSKAEAEERALELLEKVGLADKADAYP-------AQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267510758 515 ADILILDEATSNIDtrTELqIQEGLnNLMR-----GRTSFVIAHRLKTIEK-ADQILVIKDGSI 572
Cdd:cd03262 154 PKVMLFDEPTSALD--PEL-VGEVL-DVMKdlaeeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
47-307 |
8.91e-28 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 113.38 E-value: 8.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 47 IFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTA-----RMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDIF 121
Cdd:cd18573 2 LALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFglslkTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 122 EKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVP---IMFFVT 198
Cdd:cd18573 82 KSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPpiaVGAVFY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 199 KKLVaysgKNFAKR-QKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNL 277
Cdd:cd18573 162 GRYV----RKLSKQvQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNL 237
|
250 260 270
....*....|....*....|....*....|
gi 1267510758 278 GMGLVIGTGSVMVLNGMTTVGVIAAFINYS 307
Cdd:cd18573 238 SLLSVLYYGGSLVASGELTVGDLTSFLMYA 267
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
362-583 |
2.28e-27 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 110.50 E-value: 2.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEENKtiLKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKeyDINSLRGKIGVVLQ 441
Cdd:cd03299 3 VENLSKDWKEFK--LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 442 DTYLFAG-TIMDNIRYG----RLDAS--DEEVINAAKAASahsfIKHLPNQYETKiasegsnLSQGQKQLLAIARAILAD 514
Cdd:cd03299 79 NYALFPHmTVYKNIAYGlkkrKVDKKeiERKVLEIAEMLG----IDHLLNRKPET-------LSGGEQQRVAIARALVVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267510758 515 ADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESLME 583
Cdd:cd03299 148 PKILLLDEPFSALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
40-325 |
5.62e-27 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 111.06 E-value: 5.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 40 KAALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSgtarmcLLLIAIYGVTVFLTWLQIFVMV-NVALKTIQK--- 115
Cdd:cd18555 1 KKLLISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLN------LLNVLGIGILILFLLYGLFSFLrGYIIIKLQTkld 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 116 --IRQDIFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPI 193
Cdd:cd18555 75 ksLMSDFFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 194 MFFV----TKKLVAYSGKNFAKRQKdlgeLNGFIEEAITG-ADVTTLyGKEKETVQNF-NKINEQLRVSaTKADTFSAFI 267
Cdd:cd18555 154 IVLLllltRKKIKKLNQEEIVAQTK----VQSYLTETLYGiETIKSL-GSEKNIYKKWeNLFKKQLKAF-KKKERLSNIL 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 268 FPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQ 325
Cdd:cd18555 228 NSISSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFI 285
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
360-576 |
5.99e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 112.11 E-value: 5.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeyDINSL----RGk 435
Cdd:COG3842 6 LELENVSKRYGDV-TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR-----DVTGLppekRN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 436 IGVVLQDtY-LFAG-TIMDNIRYG-RLDASDEEVInAAKAASA------HSFIKHLPNQyetkiasegsnLSQGQKQLLA 506
Cdd:COG3842 79 VGMVFQD-YaLFPHlTVAENVAFGlRMRGVPKAEI-RARVAELlelvglEGLADRYPHQ-----------LSGGQQQRVA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 507 IARAILADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAH------RLktiekADQILVIKDGSIIEKG 576
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRelGITFIYVTHdqeealAL-----ADRIAVMNDGRIEQVG 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
360-576 |
1.16e-26 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 107.73 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeyDINSLRGK---I 436
Cdd:cd03301 1 VELENVTKRFG-NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR-----DVTDLPPKdrdI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 437 GVVLQDTYLFAG-TIMDNIRYG-RLDASDEEVINAAKAASAHSF-IKHLPNQYETKiasegsnLSQGQKQLLAIARAILA 513
Cdd:cd03301 75 AMVFQNYALYPHmTVYDNIAFGlKLRKVPKDEIDERVREVAELLqIEHLLDRKPKQ-------LSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267510758 514 DADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAH-RLKTIEKADQILVIKDGSIIEKG 576
Cdd:cd03301 148 EPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
360-572 |
1.40e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 111.32 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeyDINSL----RGk 435
Cdd:COG3839 4 LELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGR-----DVTDLppkdRN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 436 IGVVLQDtylFA----GTIMDNIRYG----RLDAS--DEEVINAAKAASAHSFIKHLPNQyetkiasegsnLSQGQKQLL 505
Cdd:COG3839 77 IAMVFQS---YAlyphMTVYENIAFPlklrKVPKAeiDRRVREAAELLGLEDLLDRKPKQ-----------LSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 506 AIARAILADADILILDEATSNID------TRTEL-QIQEGLNnlmrgrTSFVIA-H------RLktiekADQILVIKDGS 571
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDaklrveMRAEIkRLHRRLG------TTTIYVtHdqveamTL-----ADRIAVMNDGR 211
|
.
gi 1267510758 572 I 572
Cdd:COG3839 212 I 212
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
40-574 |
2.93e-26 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 112.97 E-value: 2.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 40 KAALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGT-ARMCLLLIAIYGVTVFLTwlQIfVMVNVALKTIQKIRQ 118
Cdd:COG4615 9 RESRWLLLLALLLGLLSGLANAGLIALINQALNATGAALARlLLLFAGLLVLLLLSRLAS--QL-LLTRLGQHAVARLRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 119 DIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALtQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVT 198
Cdd:COG4615 86 RLSRRILAAPLERLERIGAARLLAALTEDVRTISQAF-VRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLGVAGY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 199 KKLVAYSGKNFAK-RQKDlGELNGFIEEAITGAdvttlygkeKETvqnfnKIN----------------EQLRVSATKAD 261
Cdd:COG4615 165 RLLVRRARRHLRRaREAE-DRLFKHFRALLEGF---------KEL-----KLNrrrrraffdedlqptaERYRDLRIRAD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 262 TFSAFIFPSMNFINNLGMGLVIGtgsVMVLNGMTTVGVIAAF---INYSRQfsrPLSQFATLMNTI-QAAVAGG--ERVF 335
Cdd:COG4615 230 TIFALANNWGNLLFFALIGLILF---LLPALGWADPAVLSGFvlvLLFLRG---PLSQLVGALPTLsRANVALRkiEELE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 336 EIMDEVPEIKNKKDAFVVQNLQGHVALENVSFGYEENKT----ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYD 411
Cdd:COG4615 304 LALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 412 IQQGQIHIDGKNIKEYDINSLRGKIGVVLQDTYLFagtimDNIrYGRLDASDEEVINAakaasahsFIKHLpnQYETKIA 491
Cdd:COG4615 384 PESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF-----DRL-LGLDGEADPARARE--------LLERL--ELDHKVS 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 492 SEG-----SNLSQGQKQLLAIARAILADADILILDEATSNIDTR------TELqiqegLNNLM-RGRTSFVIAHRLKTIE 559
Cdd:COG4615 448 VEDgrfstTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEfrrvfyTEL-----LPELKaRGKTVIAISHDDRYFD 522
|
570
....*....|....*
gi 1267510758 560 KADQILVIKDGSIIE 574
Cdd:COG4615 523 LADRVLKMDYGKLVE 537
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
362-582 |
3.33e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 107.15 E-value: 3.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEEnktILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDInSLRgKIGVVLQ 441
Cdd:COG3840 4 LDDLTYRYGD---FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP-AER-PVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 442 DTYLFAG-TIMDNIRYG-----RLDASD-EEVINAAKAASAHSFIKHLPNQyetkiasegsnLSQGQKQLLAIARAILAD 514
Cdd:COG3840 79 ENNLFPHlTVAQNIGLGlrpglKLTAEQrAQVEQALERVGLAGLLDRLPGQ-----------LSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267510758 515 ADILILDEATSNIDT--RTEL-----QIQEGlnnlmRGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESLM 582
Cdd:COG3840 148 RPILLLDEPFSALDPalRQEMldlvdELCRE-----RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
360-574 |
3.38e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 107.82 E-value: 3.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKtILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQ-----QGQIHIDGKNI--KEYDINSL 432
Cdd:COG1117 12 IEVRNLNVYYGDKQ-ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIpgarvEGEILLDGEDIydPDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 433 RGKIGVVLQDTYLFAGTIMDNIRYG-RL------DASDEEVINAAKAAsahsfikHLPNQYETKIASEGSNLSQGQKQLL 505
Cdd:COG1117 91 RRRVGMVFQKPNPFPKSIYDNVAYGlRLhgikskSELDEIVEESLRKA-------ALWDEVKDRLKKSALGLSGGQQQRL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267510758 506 AIARAILADADILILDEATSNIDTRTELQIQEGLNNLmRGRTSFVI-------AHRLktiekADQILVIKDGSIIE 574
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL-KKDYTIVIvthnmqqAARV-----SDYTAFFYLGELVE 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
376-585 |
5.57e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.65 E-value: 5.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGkniKEYDINS----LRGKIGVVLQDTYLFAG-TI 450
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRFRSprdaQAAGIAIIHQELNLVPNlSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 451 MDNI-------RYGRLDasDEEVINAAKAAsahsfIKHL-----PNqyeTKIasegSNLSQGQKQLLAIARAILADADIL 518
Cdd:COG1129 97 AENIflgreprRGGLID--WRAMRRRAREL-----LARLgldidPD---TPV----GDLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267510758 519 ILDEATSNIdTRTELQIqegLNNLMR-----GRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESLMEDR 585
Cdd:COG1129 163 ILDEPTASL-TEREVER---LFRIIRrlkaqGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAELTEDE 231
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
46-307 |
9.14e-26 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 107.57 E-value: 9.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 46 VIFLVFVTTLLGLLgPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDIFEKIQ 125
Cdd:cd18575 2 LIALLIAAAATLAL-GQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 126 TLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPI----MFFVTKKL 201
Cdd:cd18575 81 RLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLvvlpIILFGRRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 202 VAYSgknfAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGL 281
Cdd:cd18575 161 RRLS----RASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVF 236
|
250 260
....*....|....*....|....*.
gi 1267510758 282 VIGTGSVMVLNGMTTVGVIAAFINYS 307
Cdd:cd18575 237 VLWLGAHDVLAGRMSAGELSQFVFYA 262
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
362-584 |
1.19e-25 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 105.21 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEENkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI---KEYDINslRGKIGV 438
Cdd:cd03224 3 VENLNAGYGKS-QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItglPPHERA--RAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 439 VLQDTYLFAG-TIMDNIR---YGRLDASDEEVINAAKAAsahsfikhLPNQYEtKIASEGSNLSQGQKQLLAIARAILAD 514
Cdd:cd03224 80 VPEGRRIFPElTVEENLLlgaYARRRAKRKARLERVYEL--------FPRLKE-RRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267510758 515 ADILILDEATSNIDTRTELQIQEGLNNL-MRGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESLMED 584
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELrDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
36-344 |
1.43e-25 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 107.54 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 36 MGYQKAALTFVIFLVFVTTLLGLLGP---YLMGVIIDQYIVPKD---LSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVA 109
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPvfaILFSKLISVFSLPDDdelRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 110 LKTIQKIRQDIFEKIqtlsLR----FFD--VRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFI-GVTIAmFALDWI 182
Cdd:cd18578 81 ERLTRRLRKLAFRAI----LRqdiaWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVaGLIIA-FVYGWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 183 LAIVTLITVPIMFFVTKKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADT 262
Cdd:cd18578 156 LALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 263 FSAFIFPSMNFINNLGMGLVIGTGSVMVLNG-MTTVGVIAAF--INYSRQFsrpLSQFATLMNTIQAAVAGGERVFEIMD 339
Cdd:cd18578 236 ISGLGFGLSQSLTFFAYALAFWYGGRLVANGeYTFEQFFIVFmaLIFGAQS---AGQAFSFAPDIAKAKAAAARIFRLLD 312
|
....*
gi 1267510758 340 EVPEI 344
Cdd:cd18578 313 RKPEI 317
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
360-583 |
1.47e-25 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 105.40 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINslRGKIGVV 439
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQDTYLFAG-TIMDNIRYG-RLDASDEEVINaAKAASAHSFIKHLpnQYETKIASEgsnLSQGQKQLLAIARAILADADI 517
Cdd:cd03300 78 FQNYALFPHlTVFENIAFGlRLKKLPKAEIK-ERVAEALDLVQLE--GYANRKPSQ---LSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267510758 518 LILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAH-RLKTIEKADQILVIKDGSIIEKGNHESLME 583
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
360-582 |
1.80e-25 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 105.55 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRfyDIQQG---QIHIDGKNIKEYDINSLRGKI 436
Cdd:COG1119 4 LELRNVTVRRGG-KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG--DLPPTygnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 437 GVV---LQDTYL------------FAGTImdniryGRLDASDEEVINAAKAASAHSFIKHLPNQ-YETkiasegsnLSQG 500
Cdd:COG1119 81 GLVspaLQLRFPrdetvldvvlsgFFDSI------GLYREPTDEQRERARELLELLGLAHLADRpFGT--------LSQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 501 QKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMR-GRTSFV-IAHRLKTI-EKADQILVIKDGSIIEKGN 577
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAeGAPTLVlVTHHVEEIpPGITHVLLLKDGRVVAAGP 226
|
....*
gi 1267510758 578 HESLM 582
Cdd:COG1119 227 KEEVL 231
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
373-573 |
3.16e-25 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 104.12 E-value: 3.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 373 KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKeYDINSLRGKIGVVLQDTYLFAG-TIM 451
Cdd:cd03263 15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGYCPQFDALFDElTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 452 DNIR-YGRLDASDEEVINaakaASAHSFIKHL-PNQYETKIAsegSNLSQGQKQLLAIARAILADADILILDEATSNIDT 529
Cdd:cd03263 94 EHLRfYARLKGLPKSEIK----EEVELLLRVLgLTDKANKRA---RTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1267510758 530 RTELQIQEGLNNLMRGRTSFVIAHRLKTIEK-ADQILVIKDGSII 573
Cdd:cd03263 167 ASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
373-576 |
3.23e-25 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 103.01 E-value: 3.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 373 KTILKEVSLKARPGETIALVGPTGSGKTTIINLLT--RFYDIQQGQIHIDGKNIkeyDINSLRGKIGVVLQDTYLFAG-T 449
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHPTlT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 450 IMDNIRYgrldasdeevinaakaasahsfikhlpnqyetkiASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDT 529
Cdd:cd03213 99 VRETLMF----------------------------------AAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1267510758 530 RTELQIQEGLNNLMR-GRTSFVIAHRLKT--IEKADQILVIKDGSIIEKG 576
Cdd:cd03213 145 SSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
376-583 |
5.05e-25 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 104.65 E-value: 5.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRG----KIGVVLQDTYLFAG-TI 450
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 451 MDNIRYGRLDASDEEVINAAKAASA------HSFIKHLPNQyetkiasegsnLSQGQKQLLAIARAILADADILILDEAT 524
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEAlelvglEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267510758 525 SNIDTRTELQIQEGLNNL--MRGRTSFVIAHRL-KTIEKADQILVIKDGSIIEKGNHESLME 583
Cdd:cd03294 189 SALDPLIRREMQDELLRLqaELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
360-584 |
1.99e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 103.34 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKT-ILKEVSLKARPGETIALVGPTGSGKTTI---INLLTRFYDIQQGQIHIDGKNIKEYDINSLRGK 435
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTIsklINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 436 IGVVLQ--DTYLFAGTIMDNIRYG---RLDASDEEVINAAKAASAHSFIKHlpnqyetkIASEGSNLSQGQKQLLAIARA 510
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFGlenRAVPRPEMIKIVRDVLADVGMLDY--------IDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267510758 511 ILADADILILDEATSNIDTRTELQIQEGLNNLM--RGRTSFVIAHRLKTIEKADQILVIKDGSIIEKGNHESLMED 584
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
40-334 |
2.43e-24 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 103.44 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 40 KAALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQD 119
Cdd:cd18782 1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 120 IFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTK 199
Cdd:cd18782 81 IIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 200 kLVAYSGKNFAKRQKDL-GELNGFIEEAITGADVTTLYGKEKETVQNF-----NKINEQLRVSATKAdTFSAFIFpsmnF 273
Cdd:cd18782 160 -LFGPILRRQIRRRAEAsAKTQSYLVESLTGIQTVKAQNAELKARWRWqnryaRSLGEGFKLTVLGT-TSGSLSQ----F 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267510758 274 INNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18782 234 LNKLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
372-576 |
2.71e-24 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 100.75 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 372 NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKeyDINSLRGKIGVVLQDTYLFAG-TI 450
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIGALIEAPGFYPNlTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 451 MDNIR-----YGRLDASDEEVINaakaasahsfIKHLPNQYETKIASegsnLSQGQKQLLAIARAILADADILILDEATS 525
Cdd:cd03268 90 RENLRllarlLGIRKKRIDEVLD----------VVGLKDSAKKKVKG----FSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1267510758 526 NIDTRTELQIQEGLNNLMR-GRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKG 576
Cdd:cd03268 156 GLDPDGIKELRELILSLRDqGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
376-576 |
2.78e-24 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 101.74 E-value: 2.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI---KEYDINslRGKIGVVLQDTYLFAG-TIM 451
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItglPPHEIA--RLGIGRTFQIPRLFPElTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 452 DNIRYGRLDASDEEVINAAKAAS-------AHSFIK--HLPNQYETKIAsegsNLSQGQKQLLAIARAILADADILILDE 522
Cdd:cd03219 94 ENVMVAAQARTGSGLLLARARREerearerAEELLErvGLADLADRPAG----ELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 523 ATS--NIDTRTEL-QIQEGLNNlmRGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKG 576
Cdd:cd03219 170 PAAglNPEETEELaELIRELRE--RGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEG 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
364-584 |
4.54e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.08 E-value: 4.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 364 NVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKeYDINSL---RGKIGVVL 440
Cdd:PRK13639 6 DLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLlevRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 441 Q--DTYLFAGTIMDNIRYGRL------DASDEEVINAAKAASAHSFIKHLPNqyetkiasegsNLSQGQKQLLAIARAIL 512
Cdd:PRK13639 85 QnpDDQLFAPTVEEDVAFGPLnlglskEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267510758 513 ADADILILDEATSNIDTRTELQIQEGLNNLMR-GRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESLMED 584
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKeGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
362-569 |
6.90e-24 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 99.86 E-value: 6.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEyDINSLRGKIGVVLQ 441
Cdd:COG4133 5 AENLSCRRGE-RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 442 DTYLFAG-TIMDNIRY----GRLDASDEEVINAAKAASAHSFIkHLPnqyetkiaseGSNLSQGQKQLLAIARAILADAD 516
Cdd:COG4133 83 ADGLKPElTVRENLRFwaalYGLRADREAIDEALEAVGLAGLA-DLP----------VRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1267510758 517 ILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIA-HRLKTIEkADQILVIKD 569
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELA-AARVLDLGD 204
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
362-577 |
1.03e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 101.28 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEEN----KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI--KEYDINSLRGK 435
Cdd:PRK13637 5 IENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 436 IGVVLQ--DTYLFAGTIMDNIRYG--RLDASDEEVINAAKAAsahsfIKHLPNQYETKIASEGSNLSQGQKQLLAIARAI 511
Cdd:PRK13637 85 VGLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEIENRVKRA-----MNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267510758 512 LADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGN 577
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
115-581 |
1.75e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 105.83 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 115 KIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTL------ 188
Cdd:PLN03232 371 RLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLfgslil 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 189 -ITVPIMFFVTKKLVAYSGKNFAKRQKDLGELNgfieEAITGADVTTLYGKEKETVQNFNKI-NEQLRV--SATKADTFS 264
Cdd:PLN03232 451 fLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIIN----EILASMDTVKCYAWEKSFESRIQGIrNEELSWfrKAQLLSAFN 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 265 AFIFPSMNFINNLgmglvIGTGSVMVLNGMTTVGviAAFINYS--RQFSRPLSQFATLMNTIQAAVAGGERVFE------ 336
Cdd:PLN03232 527 SFILNSIPVVVTL-----VSFGVFVLLGGDLTPA--RAFTSLSlfAVLRSPLNMLPNLLSQVVNANVSLQRIEElllsee 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 337 -IMDEVPEIKNKKDAFVVQNlqghvalENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTrfydiqqG 415
Cdd:PLN03232 600 rILAQNPPLQPGAPAISIKN-------GYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML-------G 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 416 QI-HIDGKNIkeydinSLRGKIGVVLQDTYLFAGTIMDNIRYGRlDASDEEVINAAKAASAHSFIKHLPNQYETKIASEG 494
Cdd:PLN03232 666 ELsHAETSSV------VIRGSVAYVPQVSWIFNATVRENILFGS-DFESERYWRAIDVTALQHDLDLLPGRDLTEIGERG 738
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 495 SNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEG-LNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSII 573
Cdd:PLN03232 739 VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIK 818
|
....*...
gi 1267510758 574 EKGNHESL 581
Cdd:PLN03232 819 EEGTFAEL 826
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
360-572 |
3.82e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 99.42 E-value: 3.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKT--ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIG 437
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 438 VVLQ--DTYLFAGTIMDNIRYG------RLDASDEEVINAAKAASAHSFIKHLPnqyetkiasegSNLSQGQKQLLAIAR 509
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFGlenkgiPHEEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267510758 510 AILADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTIEKADQILVIKDGSI 572
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
360-573 |
4.29e-23 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 95.96 E-value: 4.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENV--SFGyeeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikEYDINS----LR 433
Cdd:cd03216 1 LELRGItkRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK---EVSFASprdaRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 434 GKIGVVLQdtylfagtimdnirygrldasdeevinaakaasahsfikhlpnqyetkiasegsnLSQGQKQLLAIARAILA 513
Cdd:cd03216 75 AGIAMVYQ-------------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267510758 514 DADILILDEATSNIDTRtelQIQEgLNNLMR-----GRTSFVIAHRLKTI-EKADQILVIKDGSII 573
Cdd:cd03216 100 NARLLILDEPTAALTPA---EVER-LFKVIRrlraqGVAVIFISHRLDEVfEIADRVTVLRDGRVV 161
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
360-584 |
8.75e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 97.47 E-value: 8.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVS--FGyeeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIK--EYDINSLRGK 435
Cdd:PRK09493 2 IEFKNVSkhFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 436 IGVVLQDTYLFAG-TIMDNIRYGRLD---ASDEEVINAAK--------AASAHsfikHLPnqyetkiasegSNLSQGQKQ 503
Cdd:PRK09493 79 AGMVFQQFYLFPHlTALENVMFGPLRvrgASKEEAEKQARellakvglAERAH----HYP-----------SELSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 504 LLAIARAILADADILILDEATSNIDtrTELQiQEGLnNLMR-----GRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGN 577
Cdd:PRK09493 144 RVAIARALAVKPKLMLFDEPTSALD--PELR-HEVL-KVMQdlaeeGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGD 219
|
....*..
gi 1267510758 578 HESLMED 584
Cdd:PRK09493 220 PQVLIKN 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
362-582 |
1.38e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.39 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVLQ 441
Cdd:PRK11231 5 TENLTVGYG-TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 442 DTYLFAG-TIMDNIRYGR---------LDASDEEVINAAKAASAhsfIKHLPNQYETkiasegsNLSQGQKQLLAIARAI 511
Cdd:PRK11231 84 HHLTPEGiTVRELVAYGRspwlslwgrLSAEDNARVNQAMEQTR---INHLADRRLT-------DLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267510758 512 LADADILILDEATSNIDtrteLQIQEGLNNLMR-----GRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESLM 582
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLD----INHQVELMRLMRelntqGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVM 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
362-576 |
1.38e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 99.45 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGkniKEYDIN--SLRGKIGVV 439
Cdd:COG1118 5 VRNISKRFG-SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG---RDLFTNlpPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQDTYLFAG-TIMDNIRYG--RLDASDEEVinAAKAAS------AHSFIKHLPNQyetkiasegsnLSQGQKQLLAIARA 510
Cdd:COG1118 81 FQHYALFPHmTVAENIAFGlrVRPPSKAEI--RARVEEllelvqLEGLADRYPSQ-----------LSGGQRQRVALARA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267510758 511 ILADADILILDEATSNIDT--RTELQIQeglnnLMR-----GRTS-FVI-----AHRLktiekADQILVIKDGSIIEKG 576
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAkvRKELRRW-----LRRlhdelGGTTvFVThdqeeALEL-----ADRVVVMNQGRIEQVG 216
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
374-573 |
2.05e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 97.03 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 374 TILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI---KEYDINSLrgkiGVV--LQDTYLFAG 448
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglPPHRIARL----GIArtFQNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 449 -TIMDNIRYGRLDASDEEVINAA----------KAASAHSF-------IKHLPNQYetkiaseGSNLSQGQKQLLAIARA 510
Cdd:COG0411 94 lTVLENVLVAAHARLGRGLLAALlrlprarreeREARERAEellervgLADRADEP-------AGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267510758 511 ILADADILILDEATS--NIDTRTEL-----QIQEGlnnlmRGRTSFVIAHRLKTIEK-ADQILVIKDGSII 573
Cdd:COG0411 167 LATEPKLLLLDEPAAglNPEETEELaelirRLRDE-----RGITILLIEHDMDLVMGlADRIVVLDFGRVI 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
369-577 |
2.45e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 96.38 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 369 YEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQ-----QGQIHIDGKNI--KEYDINSLRGKIGVVLQ 441
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 442 DTYLFAGTIMDNIRYG-RLDA-SDEEVINAA-----KAASahsfikhLPNQYETKIASEGSNLSQGQKQLLAIARAILAD 514
Cdd:PRK14239 94 QPNPFPMSIYENVVYGlRLKGiKDKQVLDEAvekslKGAS-------IWDEVKDRLHDSALGLSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267510758 515 ADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGN 577
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYND 230
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
40-311 |
3.68e-22 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 97.15 E-value: 3.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 40 KAALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQD 119
Cdd:cd18567 1 KRALLQILLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 120 IFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVtk 199
Cdd:cd18567 81 LFRHLLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALL-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 200 KLVAYSgknfakRQKDLGEL--------NGFIEEAITGADVTTLYGKEKE---TVQNF--NKINEQLRVSatKADTFSAF 266
Cdd:cd18567 158 RLALYP------PLRRATEEqivasakeQSHFLETIRGIQTIKLFGREAEreaRWLNLlvDAINADIRLQ--RLQILFSA 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1267510758 267 IfpsMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFS 311
Cdd:cd18567 230 A---NGLLFGLENILVIYLGALLVLDGEFTVGMLFAFLAYKDQFS 271
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
360-577 |
5.00e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.87 E-value: 5.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKtILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQ-----QGQIHIDGKNIKE--YDINSL 432
Cdd:PRK14258 8 IKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYErrVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 433 RGKIGVVLQDTYLFAGTIMDNIRYG--------RLDAsDEEVINAAKAASAHSFIKHlpnqyetKIASEGSNLSQGQKQL 504
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYGvkivgwrpKLEI-DDIVESALKDADLWDEIKH-------KIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267510758 505 LAIARAILADADILILDEATSNIDTRTELQIQEGLNNL-MRGRTSFVI-AHRLKtiekadQILVIKDGSIIEKGN 577
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrLRSELTMVIvSHNLH------QVSRLSDFTAFFKGN 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
379-584 |
6.20e-22 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 97.05 E-value: 6.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 379 VSLKARPGETIALVGPTGSGKTTIINLLTRFYD---IQQGQIHIDGKNI---KEYDINSLRGK-IGVVLQDTYlfagT-- 449
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLlklSEKELRKIRGReIQMIFQDPM----Tsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 450 ---------IMDNIRYGRlDASDEEVINAAKAA-------SAHSFIKHLPNQyetkiasegsnLSQGQKQLLAIARAILA 513
Cdd:COG0444 100 npvmtvgdqIAEPLRIHG-GLSKAEARERAIELlervglpDPERRLDRYPHE-----------LSGGMRQRVMIARALAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267510758 514 DADILILDEATSNIDTRTELQIQEGLNNLMRGR-TSFV-IAHRLKTIEK-ADQILVIKDGSIIEKGNHESLMED 584
Cdd:COG0444 168 EPKLLIADEPTTALDVTIQAQILNLLKDLQRELgLAILfITHDLGVVAEiADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
359-577 |
7.47e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 97.07 E-value: 7.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 359 HVALENVSFGYEENK---TILKEVSLKARPGETIALVGPTGSGKTT---IINLLTRFydiQQGQIHIDGKNIKEYDINSL 432
Cdd:COG1135 1 MIELENLSKTFPTKGgpvTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLERP---TSGSVLVDGVDLTALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 433 RG---KIGVVLQDTYLFAG-TIMDNIRYG-RLDASDEEVInAAKAAS----------AHSFikhlPNQyetkiasegsnL 497
Cdd:COG1135 78 RAarrKIGMIFQHFNLLSSrTVAENVALPlEIAGVPKAEI-RKRVAEllelvglsdkADAY----PSQ-----------L 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 498 SQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGSIIE 574
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
...
gi 1267510758 575 KGN 577
Cdd:COG1135 222 QGP 224
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
46-334 |
9.29e-22 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 95.78 E-value: 9.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 46 VIFLVfVTTLLGLLGPYLMGVIIDqyIVPKDLSGT--------ARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIR 117
Cdd:cd18780 2 TIALL-VSSGTNLALPYFFGQVID--AVTNHSGSGgeealralNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 118 QDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFV 197
Cdd:cd18780 79 KRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 198 TkklVAYSG--KNFAKRQKD-LGELNGFIEEAITGADVTTLYGKEKETVQNFN-KINEQLRVSATKADTFSAFiFPSMNF 273
Cdd:cd18780 159 A---VIYGKyvRKLSKKFQDaLAAASTVAEESISNIRTVRSFAKETKEVSRYSeKINESYLLGKKLARASGGF-NGFMGA 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267510758 274 INNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18780 235 AAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
363-556 |
9.35e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 95.23 E-value: 9.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 363 ENVSFgYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDI-----QQGQIHIDGKNIKEYDIN--SLRGK 435
Cdd:PRK14243 14 ENLNV-YYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYAPDVDpvEVRRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 436 IGVVLQDTYLFAGTIMDNIRYG-RLDAS----DEEVINAAKAASahsfikhLPNQYETKIASEGSNLSQGQKQLLAIARA 510
Cdd:PRK14243 93 IGMVFQKPNPFPKSIYDNIAYGaRINGYkgdmDELVERSLRQAA-------LWDEVKDKLKQSGLSLSGGQQQRLCIARA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1267510758 511 ILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLK 556
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQ 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
362-524 |
1.03e-21 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 94.28 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEENkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeyDINSL-------RG 434
Cdd:COG0410 6 VENLHAGYGGI-HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGE-----DITGLpphriarLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 435 kIGVVLQDTYLFAG-TIMDNIRYGRLDASDEEVINAAKAASAHSFikhlPNQYEtKIASEGSNLSQGQKQLLAIARAILA 513
Cdd:COG0410 80 -IGYVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADLERVYELF----PRLKE-RRRQRAGTLSGGEQQMLAIGRALMS 153
|
170
....*....|.
gi 1267510758 514 DADILILDEAT 524
Cdd:COG0410 154 RPKLLLLDEPS 164
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
360-572 |
2.81e-21 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 92.47 E-value: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYD---INSLRGKI 436
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 437 GVVLQDTYLFAG-TIMDNIRYGR--LDASDEEVINAAKAASAHSFIKHlpnqyetKIASEGSNLSQGQKQLLAIARAILA 513
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAFALevTGVPPREIRKRVPAALELVGLSH-------KHRALPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267510758 514 DADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQ--ILVIKDGSI 572
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
360-581 |
2.89e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 94.01 E-value: 2.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDI-----QQGQIHIDGKNIKEY-DINSLR 433
Cdd:PRK14271 22 MAAVNLTLGFA-GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLEFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 434 GKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILA 513
Cdd:PRK14271 101 RRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267510758 514 DADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESL 581
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
362-574 |
3.02e-21 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 97.74 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVLQ 441
Cdd:PRK10522 325 LRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 442 DTYLFagtimdniryGRLDASDEEvinAAKAASAHSFIKHLpnQYETKIASEGS-----NLSQGQKQLLAIARAILADAD 516
Cdd:PRK10522 405 DFHLF----------DQLLGPEGK---PANPALVEKWLERL--KMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 517 ILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTIEKADQILVIKDGSIIE 574
Cdd:PRK10522 470 ILLLDEWAADQDPHFRREFYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
376-584 |
3.43e-21 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 97.45 E-value: 3.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 376 LKEVSLKARPGETIALVGPTGSGKTT----IINLLTrfydiQQGQIHIDGKNI---KEYDINSLRGKIGVVLQDTYlfaG 448
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLIP-----SEGEIRFDGQDLdglSRRALRPLRRRMQVVFQDPF---G 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 449 ------TIMDNIRYG------RLDASD-EEVINAA------KAASAHSFikhlPNQyetkiasegsnLSQGQKQLLAIAR 509
Cdd:COG4172 374 slsprmTVGQIIAEGlrvhgpGLSAAErRARVAEAleevglDPAARHRY----PHE-----------FSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 510 AILADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESLMED 584
Cdd:COG4172 439 ALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQRehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
375-585 |
3.73e-21 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 93.77 E-value: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 375 ILKEVSLKARPGETIALVGPTGSGKTTIINLLTrfydiqqGQIHIDGKNIKEydinslRGKIGVVLQDTYLFAGTIMDNI 454
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLIL-------GELEPSEGKIKH------SGRISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 455 RYGrLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQ 534
Cdd:cd03291 119 IFG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKE 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1267510758 535 IQEG-LNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKGNHESLMEDR 585
Cdd:cd03291 198 IFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
43-571 |
5.68e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 96.80 E-value: 5.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 43 LTFVIFLVFVTTLLGLLGPYLMGVIIDQyIVPKDLSG----TARMCLLLIAIYGVTVFLTWLQifvmvnvalktiqkirq 118
Cdd:COG4178 27 LALLLLLTLASVGLNVLLNFWNRDFYDA-LQARDAAAfwqqLGVFALLAAISILLAVYQTYLR----------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 119 difekiQTLSLR------------------FFDVRSQGDLMS----RVTNDIDNL-NQALT------QSVVQIIS----- 164
Cdd:COG4178 89 ------QRLQIRwrewlterlldrwlsnraYYRLQLSGGEIDnpdqRIAEDIRLFtETTLSlslgllSSVVTLISfigil 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 165 ------SALTFIGVTIA----MFaldWILAIVTLITVPIMFFVTKKLVaysGKNFAKRQK--DL-GEL-----NGfieEA 226
Cdd:COG4178 163 wslsgsLTFTLGGYSITipgyMV---WAALIYAIIGTLLTHLIGRPLI---RLNFEQQRReaDFrFALvrvreNA---ES 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 227 ITgadvttLYGKEKE-----------TVQNFNK-INEQLRVSA-TKADTFSAFIFPSmnfinnlgmgLVIgtgSVMVLNG 293
Cdd:COG4178 234 IA------LYRGEAAerrrlrrrfdaVIANWRRlIRRQRNLTFfTTGYGQLAVIFPI----------LVA---APRYFAG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 294 MTTVGVI----AAFinysRQFSRPLSQFATLMNTIQAAVAGGERV--FEIMDEVPEIKNKKDAFVVQNLQGHVALENVSF 367
Cdd:COG4178 295 EITLGGLmqaaSAF----GQVQGALSWFVDNYQSLAEWRATVDRLagFEEALEAADALPEAASRIETSEDGALALEDLTL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 368 GYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHI-DGKNIkeydinslrgkigVVL-QDTYL 445
Cdd:COG4178 371 RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-------------LFLpQRPYL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 446 FAGTIMDNIRY--GRLDASDEEVINAAKAASahsfIKHLPNQYETKiASEGSNLSQGQKQLLAIARAILADADILILDEA 523
Cdd:COG4178 438 PLGTLREALLYpaTAEAFSDAELREALEAVG----LGHLAERLDEE-ADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1267510758 524 TSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGS 571
Cdd:COG4178 513 TSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
376-576 |
7.34e-21 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 91.28 E-value: 7.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGknikeYDINS----LRGKIGVVLQDTYLFAG-TI 450
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-----FDVVKepaeARRRLGFVSDSTGLYDRlTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 451 MDNIRY-GRLdasdeeviNAAKAASAHSFIKHLPNQYETK--IASEGSNLSQGQKQLLAIARAILADADILILDEATSNI 527
Cdd:cd03266 96 RENLEYfAGL--------YGLKGDELTARLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1267510758 528 D---TRTELQIQEGLNNLmrGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKG 576
Cdd:cd03266 168 DvmaTRALREFIRQLRAL--GKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
385-576 |
8.71e-21 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 91.20 E-value: 8.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 385 PGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDG-------KNIkeyDINSLRGKIGVVLQDTYLFAG-TIMDNIRY 456
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKI---NLPPQQRKIGLVFQQYALFPHlNVRENLAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 457 GRLDASDEEVINAAKAASAHSFIKHLPNQYETKiasegsnLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQ 536
Cdd:cd03297 99 GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQ-------LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1267510758 537 EGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKG 576
Cdd:cd03297 172 PELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
364-572 |
1.65e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 93.22 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 364 NVSFGyeeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeyDINSLRGK---IGVVL 440
Cdd:PRK10851 9 KKSFG---RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT-----DVSRLHARdrkVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 441 QDTYLFAG-TIMDNIRYG-----RLDASDEEVINaAKAASAHSFIK--HLPNQYEtkiasegSNLSQGQKQLLAIARAIL 512
Cdd:PRK10851 81 QHYALFRHmTVFDNIAFGltvlpRRERPNAAAIK-AKVTQLLEMVQlaHLADRYP-------AQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 513 ADADILILDEATSNIDT--RTEL-----QIQEGLNnlmrgRTS-FVIAHRLKTIEKADQILVIKDGSI 572
Cdd:PRK10851 153 VEPQILLLDEPFGALDAqvRKELrrwlrQLHEELK-----FTSvFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
360-576 |
1.84e-20 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 89.86 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKTILkevSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINslRGKIGVV 439
Cdd:cd03298 1 VRLDKIRFSYGEQPMHF---DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQDTYLFAG-TIMDNIRYG-----RLDASDEEVINAAKAASA-HSFIKHLPNQyetkiasegsnLSQGQKQLLAIARAIL 512
Cdd:cd03298 76 FQENNLFAHlTVEQNVGLGlspglKLTAEDRQAIEVALARVGlAGLEKRLPGE-----------LSGGERQRVALARVLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267510758 513 ADADILILDEATSNIDTRTELQIQEGLNNL--MRGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKG 576
Cdd:cd03298 145 RDKPVLLLDEPFAALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
360-584 |
2.16e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 95.96 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEE--NKTILKEVSLKARPGETIALVGPTGSGKTTIIN-LLTRFYDIQQGQIHIdgknikeydinslRGKI 436
Cdd:PLN03130 615 ISIKNGYFSWDSkaERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVI-------------RGTV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 437 GVVLQDTYLFAGTIMDNIRYGR-LDASDEEviNAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADA 515
Cdd:PLN03130 682 AYVPQVSWIFNATVRDNILFGSpFDPERYE--RAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 516 DILILDEATSNIDTRTELQIQEG-LNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKGNHESLMED 584
Cdd:PLN03130 760 DVYIFDDPLSALDAHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNN 829
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
364-576 |
2.19e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 90.99 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 364 NVSFGyeeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVLQDT 443
Cdd:PRK13548 9 SVRLG---GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 444 YL-FAGTIMDNIRYGRLD-----ASDEEVINAAKAASAhsfIKHLPN-QYETkiasegsnLSQGQKQLLAIARAI--LAD 514
Cdd:PRK13548 86 SLsFPFTVEEVVAMGRAPhglsrAEDDALVAAALAQVD---LAHLAGrDYPQ--------LSGGEQQRVQLARVLaqLWE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267510758 515 AD----ILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIA--HRLK-TIEKADQILVIKDGSIIEKG 576
Cdd:PRK13548 155 PDgpprWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVvlHDLNlAARYADRIVLLHQGRLVADG 223
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
360-572 |
2.45e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 93.09 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKeyDINSLRGKIGVV 439
Cdd:PRK09452 15 VELRGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQDTYLFAG-TIMDNIRYG-RL-----DASDEEVINAAKAASAHSFIKHLPNQyetkiasegsnLSQGQKQLLAIARAIL 512
Cdd:PRK09452 92 FQSYALFPHmTVFENVAFGlRMqktpaAEITPRVMEALRMVQLEEFAQRKPHQ-----------LSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267510758 513 ADADILILDEATSNIDTRTELQIQEGLNNLMR--GRT-SFVIAHRLKTIEKADQILVIKDGSI 572
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITfVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
360-576 |
4.05e-20 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 89.71 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVS--FGyeeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINslRGKIG 437
Cdd:cd03296 3 IEVRNVSkrFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 438 VVLQDTYLFAG-TIMDNIRYG-RLDASDEEVINAAKAASAHSFIK-----HLPNQYEtkiasegSNLSQGQKQLLAIARA 510
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGlRVKPRSERPPEAEIRAKVHELLKlvqldWLADRYP-------AQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267510758 511 ILADADILILDEATSNIDTrtelQIQEGLNNLMR------GRTS-FVIAHRLKTIEKADQILVIKDGSIIEKG 576
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDA----KVRKELRRWLRrlhdelHVTTvFVTHDQEEALEVADRVVVMNKGRIEQVG 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
375-571 |
4.05e-20 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 95.36 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 375 ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQI-HidgknikeydinslRGKIGVVLQDTYLFAGTIMDN 453
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIkH--------------SGRISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 454 IRYGrLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTEL 533
Cdd:TIGR01271 507 IIFG-LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190
....*....|....*....|....*....|....*....
gi 1267510758 534 QIQEG-LNNLMRGRTSFVIAHRLKTIEKADQILVIKDGS 571
Cdd:TIGR01271 586 EIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGV 624
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
360-584 |
5.64e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.05 E-value: 5.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYD-INSLRGKIGV 438
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 439 VLQ--DTYLFAGTIMDNIRYG--RLDASDEEVINAAKAASAHSFIKhlpnQYETKiasEGSNLSQGQKQLLAIARAILAD 514
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGpeNLCLPPIEIRKRVDRALAEIGLE----KYRHR---SPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267510758 515 ADILILDEATSNIDTRTELQIQEGLNNLMR-GRTSFVIAHRLKTIEKADQILVIKDGSIIEKGNHESLMED 584
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
361-584 |
5.97e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.52 E-value: 5.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 361 ALENVSFG-YEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQ-----GQIHIDGKNIKEYDINSL-- 432
Cdd:PRK14267 4 AIETVNLRvYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPIev 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 433 RGKIGVVLQDTYLFAG-TIMDNI----RYGRLDAS----DEEVINAAKAASAHSFIKHLPNQYEtkiasegSNLSQGQKQ 503
Cdd:PRK14267 84 RREVGMVFQYPNPFPHlTIYDNVaigvKLNGLVKSkkelDERVEWALKKAALWDEVKDRLNDYP-------SNLSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 504 LLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHR-LKTIEKADQILVIKDGSIIEKGNHESLM 582
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
..
gi 1267510758 583 ED 584
Cdd:PRK14267 237 EN 238
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
376-588 |
6.26e-20 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 94.63 E-value: 6.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIdgknikeydinslRGKIGVVLQDTYLFAGTIMDNIR 455
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-------------KGSVAYVPQQAWIQNDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 456 YGRldASDEEVINAAKAASAH-SFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQ 534
Cdd:TIGR00957 721 FGK--ALNEKYYQQVLEACALlPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1267510758 535 IQE---GLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKGNHESLMEDRGFY 588
Cdd:TIGR00957 799 IFEhviGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
40-327 |
7.75e-20 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 90.25 E-value: 7.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 40 KAALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNvalkTIQKIrqD 119
Cdd:cd18588 1 KKLLGEVLLASLFLQLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSH----TTNRI--D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 120 ------IFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTqsvvqiiSSALT------FIGVTIA-MFALDWILAIV 186
Cdd:cd18588 75 aelgarLFRHLLRLPLSYFESRQVGDTVARV-RELESIRQFLT-------GSALTlvldlvFSVVFLAvMFYYSPTLTLI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 187 TLITVPIMF----FVTKKLvaysgKNFAKRQKDLGELN-GFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKAD 261
Cdd:cd18588 147 VLASLPLYAllslLVTPIL-----RRRLEEKFQRGAENqSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTA 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267510758 262 TFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAA 327
Cdd:cd18588 222 NLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQA 287
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
360-576 |
7.78e-20 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 88.02 E-value: 7.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEeNKTILKEVSLKARPGeTIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEyDINSLRGKIGVV 439
Cdd:cd03264 1 LQLENLTKRYG-KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQDTYLFAG-TIMDNIRY---------GRLDASDEEVINAAkaasahsfikHLPNQYETKIASegsnLSQGQKQLLAIAR 509
Cdd:cd03264 78 PQEFGVYPNfTVREFLDYiawlkgipsKEVKARVDEVLELV----------NLGDRAKKKIGS----LSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 510 AILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKG 576
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
369-581 |
8.01e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 89.34 E-value: 8.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 369 YEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHID------GKNIKEYDINSLRGKIGVVLQD 442
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 443 TYLFAG-TIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILILD 521
Cdd:PRK14246 99 PNPFPHlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267510758 522 EATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESL 581
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
362-597 |
8.32e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 88.92 E-value: 8.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEENKtILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDG------KNIKEYDINSLRGK 435
Cdd:PRK11124 5 LNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 436 IGVVLQDTYLFAG-TIMDN-----IRYgrLDASDEEVINAAK--------AASAHSFIKHlpnqyetkiasegsnLSQGQ 501
Cdd:PRK11124 84 VGMVFQQYNLWPHlTVQQNlieapCRV--LGLSKDQALARAEkllerlrlKPYADRFPLH---------------LSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 502 KQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMR-GRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHE 579
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
250
....*....|....*...
gi 1267510758 580 SLMEDRgfyfdlyTSQFK 597
Cdd:PRK11124 227 CFTQPQ-------TEAFK 237
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
360-576 |
8.76e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 88.11 E-value: 8.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINslrgKIGVV 439
Cdd:cd03269 1 LEVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN----RIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQDTYLFAG-TIMDNIRY-GRL-DASDEEVinaakAASAHSFIK--HLPNQYETKIasegSNLSQGQKQLLAIARAILAD 514
Cdd:cd03269 76 PEERGLYPKmKVIDQLVYlAQLkGLKKEEA-----RRRIDEWLErlELSEYANKRV----EELSKGNQQKVQFIAAVIHD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267510758 515 ADILILDEATSNIDTRTELQIQEGLNNLMR-GRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKG 576
Cdd:cd03269 147 PELLILDEPFSGLDPVNVELLKDVIRELARaGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
360-585 |
1.02e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 89.89 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKTI----LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIK----EYDINS 431
Cdd:PRK13641 3 IKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 432 LRGKIGVVLQ--DTYLFAGTIMDNIRYGRLD--ASDEEVINAAKaasahSFIKH--LPNQYETKIASEgsnLSQGQKQLL 505
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKAL-----KWLKKvgLSEDLISKSPFE---LSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 506 AIARAILADADILILDEATSNIDTRTELQIQEGLNNLMR-GRTSFVIAHRLKTI-EKADQILVIKDGSIIEKGNHESLME 583
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFS 234
|
..
gi 1267510758 584 DR 585
Cdd:PRK13641 235 DK 236
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
363-581 |
1.04e-19 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 88.20 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 363 ENVSFGYEENkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEyDINSLRGKIGVVLQD 442
Cdd:cd03265 4 ENLVKKYGDF-EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 443 tylfagTIMDNIrygrLDASDEEVINAAkaasahsfIKHLPNQYETKIASE--------------GSNLSQGQKQLLAIA 508
Cdd:cd03265 82 ------LSVDDE----LTGWENLYIHAR--------LYGVPGAERRERIDElldfvglleaadrlVKTYSGGMRRRLEIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267510758 509 RAILADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESL 581
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
360-574 |
1.09e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.44 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIdGKNIkeydinslrgKIGVV 439
Cdd:COG0488 316 LELEGLSKSYGD-KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQDTYLFAG--TIMDNIRYGRLDASDEEVINAAKAasahsFikhL--PNQYETKIASegsnLSQGQKQLLAIARAILADA 515
Cdd:COG0488 384 DQHQEELDPdkTVLDELRDGAPGGTEQEVRGYLGR-----F---LfsGDDAFKPVGV----LSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267510758 516 DILILDEATSN--IDTRTELqiQEGLNNLmRGrTSFVIAH-R--LKTIekADQILVIKDGSIIE 574
Cdd:COG0488 452 NVLLLDEPTNHldIETLEAL--EEALDDF-PG-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
355-577 |
1.42e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 89.30 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 355 NLQGHVALENVSFGYEENKTI----LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQ-------IHIDGKN 423
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTPFefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdyaIPANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 424 IKEydINSLRGKIGVVLQ--DTYLFAGTIMDNIRYG--RLDASDEEVInaaKAASAHSFIKHLPNQYETKIASEgsnLSQ 499
Cdd:PRK13645 82 IKE--VKRLRKEIGLVFQfpEYQLFQETIEKDIAFGpvNLGENKQEAY---KKVPELLKLVQLPEDYVKRSPFE---LSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 500 GQKQLLAIARAILADADILILDEATSNIDTRTE---LQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKG 576
Cdd:PRK13645 154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEedfINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
.
gi 1267510758 577 N 577
Cdd:PRK13645 234 S 234
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
373-584 |
2.64e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 87.50 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 373 KTILKEVSLKARPGETIALVGPTGSGKTTI---INLLTRFYD--IQQGQIHIDGK---NIKEYDINSLRGKIGVVLQDTY 444
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrcINLLEQPEAgtIRVGDITIDTArslSQQKGLIRQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 445 LFAG-TIMDNIRYGRL---DASDEEVINAAKAASAHSFIKHLPNQYETKiasegsnLSQGQKQLLAIARAILADADILIL 520
Cdd:PRK11264 96 LFPHrTVLENIIEGPVivkGEPKEEATARARELLAKVGLAGKETSYPRR-------LSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 521 DEATSNIDtrTELqIQEGLNNLmRG-----RTSFVIAHRLK-TIEKADQILVIKDGSIIEKGNHESLMED 584
Cdd:PRK11264 169 DEPTSALD--PEL-VGEVLNTI-RQlaqekRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
367-574 |
3.24e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 87.82 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 367 FGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYD---INSLRGKIGVVLQDT 443
Cdd:PRK10419 19 SGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 444 yLFA----GTIMDNIR-----YGRLDASD-----EEVINAAKAASAHsfIKHLPNQyetkiasegsnLSQGQKQLLAIAR 509
Cdd:PRK10419 99 -ISAvnprKTVREIIReplrhLLSLDKAErlaraSEMLRAVDLDDSV--LDKRPPQ-----------LSGGQLQRVCLAR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 510 AILADADILILDEATSNIDTRTELQIQEGLNNLM-RGRTSFV-IAHRLKTIEK-ADQILVIKDGSIIE 574
Cdd:PRK10419 165 ALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQqQFGTACLfITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
365-576 |
3.29e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 87.28 E-value: 3.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 365 VSFGyeeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQ-----QGQIHIDGKNIKEYDINSLRGKIGVV 439
Cdd:PRK14247 11 VSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQDTYLFAG-TIMDNIRYG----RLDASDEEVINAAKAASAHSfikHLPNQYETKIASEGSNLSQGQKQLLAIARAILAD 514
Cdd:PRK14247 88 FQIPNPIPNlSIFENVALGlklnRLVKSKKELQERVRWALEKA---QLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267510758 515 ADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKG 576
Cdd:PRK14247 165 PEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWG 227
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
46-334 |
3.70e-19 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 88.00 E-value: 3.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 46 VIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSgtarmcLLLIAIYGVTVFLTWLQIFVMV--NVALKTIQKIRQDIFEK 123
Cdd:cd18568 7 ILLASLLLQLLGLALPLFTQIILDRVLVHKNIS------LLNLILIGLLIVGIFQILLSAVrqYLLDYFANRIDLSLLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 124 I--QTLSL--RFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVP----IMF 195
Cdd:cd18568 81 FykHLLSLplSFFASRKVGDIITRF-QENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPlyvlLTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 196 FVTKKLVAYSGKNFAKRQkdlgELNGFIEEAITGADVTTLYGKEKETVQNF-NKINEQL--RVSATKADTFSAFIFpsmN 272
Cdd:cd18568 160 LSSPKLKRNSREIFQANA----EQQSFLVEALTGIATIKALAAERPIRWRWeNKFAKALntRFRGQKLSIVLQLIS---S 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267510758 273 FINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18568 233 LINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
362-576 |
4.01e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 87.84 E-value: 4.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEENKTI--LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVV 439
Cdd:PRK13642 7 VENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQ--DTYLFAGTIMDNIRYGRLDAS---DEEVINAAKAASAHSFIkhlpnQYETKiasEGSNLSQGQKQLLAIARAILAD 514
Cdd:PRK13642 87 FQnpDNQFVGATVEDDVAFGMENQGiprEEMIKRVDEALLAVNML-----DFKTR---EPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267510758 515 ADILILDEATSNIDTRTELQIQEGLNNLMRGR--TSFVIAHRLKTIEKADQILVIKDGSIIEKG 576
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEA 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
372-584 |
5.91e-19 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 86.06 E-value: 5.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 372 NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDIN--SLRGkIGVVLQDTYLFAG- 448
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHkrARLG-IGYLPQEASIFRKl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 449 TIMDNIR--YGRLDASDEEVINAAKAASAHSFIKHLPNQYetkiaseGSNLSQGQKQLLAIARAILADADILILDEATSN 526
Cdd:cd03218 91 TVEENILavLEIRGLSKKEREEKLEELLEEFHITHLRKSK-------ASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 527 IDTRTELQIQEGLNNLM-RGRTSFVIAHRLK-TIEKADQILVIKDGSIIEKGNHESLMED 584
Cdd:cd03218 164 VDPIAVQDIQKIIKILKdRGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
362-585 |
6.81e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 87.38 E-value: 6.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEEN----KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI----KEYDINSLR 433
Cdd:PRK13634 5 FQKVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKPLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 434 GKIGVVLQ--DTYLFAGTIMDNIRYGRLD--ASDEEVINAAKAASAhsfIKHLPNQYETKIASEgsnLSQGQKQLLAIAR 509
Cdd:PRK13634 85 KKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIE---LVGLPEELLARSPFE---LSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267510758 510 AILADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESLMEDR 585
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKekGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
371-583 |
7.19e-19 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 91.38 E-value: 7.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 371 ENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeydinslrgkIGVVLQDTYLFAGTI 450
Cdd:PTZ00243 671 EPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS-------------IAYVPQQAWIMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 451 MDNIRYgrldaSDEEviNAAKAASA------HSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEAT 524
Cdd:PTZ00243 738 RGNILF-----FDEE--DAARLADAvrvsqlEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 525 SNIDTRT-ELQIQEGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEKGNHESLME 583
Cdd:PTZ00243 811 SALDAHVgERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
368-576 |
9.39e-19 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 85.28 E-value: 9.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 368 GYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeydINSLRGkIGVVLQDTYlfa 447
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSLLG-LGGGFNPEL--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 448 gTIMDNIR-----YGRLDASDEEVINAAKAASAhsfikhLPNQYETKIasegSNLSQGQKQLLAIARAILADADILILDE 522
Cdd:cd03220 100 -TGRENIYlngrlLGLSRKEIDEKIDEIIEFSE------LGDFIDLPV----KTYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1267510758 523 ATSNIDTRTELQIQEGLNNLM-RGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKG 576
Cdd:cd03220 169 VLAVGDAAFQEKCQRRLRELLkQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
362-561 |
9.82e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 86.29 E-value: 9.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKeyDINSLRgkiGVVLQ 441
Cdd:PRK11248 4 ISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGAER---GVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 442 DTYLFA-GTIMDNIRYGRLDASdeeVINAAKAASAHSFIKhlpnqyetKIASEGS------NLSQGQKQLLAIARAILAD 514
Cdd:PRK11248 78 NEGLLPwRNVQDNVAFGLQLAG---VEKMQRLEIAHQMLK--------KVGLEGAekryiwQLSGGQRQRVGIARALAAN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1267510758 515 ADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHrlkTIEKA 561
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITH---DIEEA 192
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
360-571 |
1.51e-18 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 84.69 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIinLLTRFYDIQ--QGQIHIDGKNIKEYDINSL----R 433
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSL--LLAILGEMQtlEGKVHWSNKNESEPSFEATrsrnR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 434 GKIGVVLQDTYLFAGTIMDNIRYGRlDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILA 513
Cdd:cd03290 79 YSVAYAAQKPWLLNATVEENITFGS-PFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267510758 514 DADILILDEATSNIDTR-TELQIQEGLNNLMRG--RTSFVIAHRLKTIEKADQILVIKDGS 571
Cdd:cd03290 158 NTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
376-587 |
1.90e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 86.29 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHI---DGKNIKEYD---------------------INS 431
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKekekvleklviqktrfkkikkIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 432 LRGKIGVVLQ--DTYLFAGTIMDNIRYG--RLDASDEEvinAAKAASAHSFIKHLPNQYETKiasEGSNLSQGQKQLLAI 507
Cdd:PRK13651 103 IRRRVGVVFQfaEYQLFEQTIEKDIIFGpvSMGVSKEE---AKKRAAKYIELVGLDESYLQR---SPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 508 ArAILA-DADILILDEATSNIDTRTELQIQEGLNNL-MRGRTSFVIAHRLKTI-EKADQILVIKDGSIIEKGNHESLMED 584
Cdd:PRK13651 177 A-GILAmEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVlEWTKRTIFFKDGKIIKDGDTYDILSD 255
|
...
gi 1267510758 585 RGF 587
Cdd:PRK13651 256 NKF 258
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
363-576 |
2.19e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.42 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 363 ENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVLQD 442
Cdd:PRK10253 11 EQLTLGYG-KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 443 TYLFAGTIMDNI----RY------GRLDASDEEVINAAKAASAhsfIKHLPNQyetkiasEGSNLSQGQKQLLAIARAIL 512
Cdd:PRK10253 90 ATTPGDITVQELvargRYphqplfTRWRKEDEEAVTKAMQATG---ITHLADQ-------SVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267510758 513 ADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRL-KTIEKADQILVIKDGSIIEKG 576
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNRekGYTLAAVLHDLnQACRYASHLIALREGKIVAQG 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
360-584 |
2.21e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 86.81 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEyDINSLRGKIGVV 439
Cdd:PRK13536 42 IDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQ-DTYLFAGTIMDNI----RYGRLDASD-EEVInaakaASAHSFIKhlpnqYETKIASEGSNLSQGQKQLLAIARAILA 513
Cdd:PRK13536 120 PQfDNLDLEFTVRENLlvfgRYFGMSTREiEAVI-----PSLLEFAR-----LESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267510758 514 DADILILDEATSNIDTRTELQIQEGLNNLM-RGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESLMED 584
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
362-577 |
2.33e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 85.93 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENV--SFGyeeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINslrgKIGvv 439
Cdd:COG4152 4 LKGLtkRFG---DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRR----RIG-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 lqdtYLFA--G-----TIMDNIRY-GRL---DASDeevinaAKAASAHSFIKH-LPNQYETKIasegSNLSQGQKQLLAI 507
Cdd:COG4152 75 ----YLPEerGlypkmKVGEQLVYlARLkglSKAE------AKRRADEWLERLgLGDRANKKV----EELSKGNQQKVQL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267510758 508 ARAILADADILILDEATS-----NIDTrtelqIQEGLNNLMR-GRTsfVI--AHRLKTIEK-ADQILVIKDGSIIEKGN 577
Cdd:COG4152 141 IAALLHDPELLILDEPFSgldpvNVEL-----LKDVIRELAAkGTT--VIfsSHQMELVEElCDRIVIINKGRKVLSGS 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
372-581 |
3.59e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.84 E-value: 3.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 372 NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDiQQGQIHIDGKNIKEYDINSL---RGKIGVVLQDTY---- 444
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPNssln 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 445 --LFAGTIMDN---IRYGRLDAS--DEEVINAAK-----AASAHSFikhlPNQYetkiasegsnlSQGQKQLLAIARAIL 512
Cdd:PRK15134 377 prLNVLQIIEEglrVHQPTLSAAqrEQQVIAVMEevgldPETRHRY----PAEF-----------SGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267510758 513 ADADILILDEATSNIDTRTELQIQEGLNNLM-RGRTSFV-IAHRLKTIEK-ADQILVIKDGSIIEKGNHESL 581
Cdd:PRK15134 442 LKPSLIILDEPTSSLDKTVQAQILALLKSLQqKHQLAYLfISHDLHVVRAlCHQVIVLRQGEVVEQGDCERV 513
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
376-585 |
3.95e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 87.68 E-value: 3.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFY--DIQQGQIHIDGKNIKEYDI-NSLRGKIGVVLQDTYLFAG-TIM 451
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphGTYEGEIIFEGEELQASNIrDTERAGIAIIHQELALVKElSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 452 DNI-------RYGRLDasDEEVINAAKAASAHSFIKHLPNqyeTKIasegSNLSQGQKQLLAIARAILADADILILDEAT 524
Cdd:PRK13549 101 ENIflgneitPGGIMD--YDAMYLRAQKLLAQLKLDINPA---TPV----GNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267510758 525 SNI---DTRTELQIQEGLNNlmRGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESLMEDR 585
Cdd:PRK13549 172 ASLtesETAVLLDIIRDLKA--HGIACIYISHKLNEVKAiSDTICVIRDGRHIGTRPAAGMTEDD 234
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
362-585 |
4.76e-18 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 83.34 E-value: 4.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEENkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeyDINSL------RGK 435
Cdd:TIGR03410 3 VSNLNVYYGQS-HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGE-----DITKLppheraRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 436 IGVVLQDTYLFAG-TIMDNIRYGrldasdeevinAAKAASAHSFIKhlPNQYE------TKIASEGSNLSQGQKQLLAIA 508
Cdd:TIGR03410 77 IAYVPQGREIFPRlTVEENLLTG-----------LAALPRRSRKIP--DEIYElfpvlkEMLGRRGGDLSGGQQQQLAIA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 509 RAILADADILILDEATSNIDTRTELQIQEGLNNL--MRGRTSFVIAHRLK-TIEKADQILVIKDGSIIEKGNHESLMEDR 585
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDfARELADRYYVMERGRVVASGAGDELDEDK 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
360-587 |
5.41e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.79 E-value: 5.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKTI----LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDG----KNIKEYDINS 431
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 432 LRGKIGVVLQ--DTYLFAGTIMDNIRYG--RLDASDEEvinAAKAASAHSFIKHLPNQYETKIASEgsnLSQGQKQLLAI 507
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGpqNFGIPKEK---AEKIAAEKLEMVGLADEFWEKSPFE---LSGGQMRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 508 ARAILADADILILDEATSNIDTRTELQIQEGLNNLMR-GRTSFVIAHRLKTI-EKADQILVIKDGSIIEKGNHESLMEDR 585
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQEV 235
|
..
gi 1267510758 586 GF 587
Cdd:PRK13643 236 DF 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
362-528 |
5.76e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.04 E-value: 5.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDgKNIkeydinslrgKIGVVLQ 441
Cdd:COG0488 1 LENLSKSFGG-RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-KGL----------RIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 442 DTYLFAG-TIMDNI------------RYGRLDAS-DEEVINAAKAASAHSFIKHLpN--QYETKIAS--EG--------- 494
Cdd:COG0488 69 EPPLDDDlTVLDTVldgdaelraleaELEELEAKlAEPDEDLERLAELQEEFEAL-GgwEAEARAEEilSGlgfpeedld 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 1267510758 495 ---SNLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:COG0488 148 rpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
362-576 |
6.39e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 85.24 E-value: 6.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEENK---TILKEVSLKARPGETIALVGPTGSGKTT---IINLLTRfydIQQGQIHIDGKNIKEYDINSLRG- 434
Cdd:PRK11153 4 LKNISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELRKa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 435 --KIGVVLQDTYLFAG-TIMDNIRYG-RLDASDEEVINAAKAA-------SAHSfikhlpNQYEtkiasegSNLSQGQKQ 503
Cdd:PRK11153 81 rrQIGMIFQHFNLLSSrTVFDNVALPlELAGTPKAEIKARVTEllelvglSDKA------DRYP-------AQLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267510758 504 LLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTI-EKADQILVIKDGSIIEKG 576
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQG 223
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
370-574 |
7.14e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 82.90 E-value: 7.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 370 EENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDIN---SLRGK-IGVVLQdTYL 445
Cdd:PRK10584 20 EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRAKhVGFVFQ-SFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 446 FAGTI--MDNIRYGRL--DASDEEVINAAKAASAH----SFIKHLPNQyetkiasegsnLSQGQKQLLAIARAILADADI 517
Cdd:PRK10584 99 LIPTLnaLENVELPALlrGESSRQSRNGAKALLEQlglgKRLDHLPAQ-----------LSGGEQQRVALARAFNGRPDV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1267510758 518 LILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTIEKADQILVIKDGSIIE 574
Cdd:PRK10584 168 LFADEPTGNLDRQTGDKIADLLFSLNRehGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
46-256 |
7.40e-18 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 84.38 E-value: 7.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 46 VIFLVFVTTLLGLLGPYLMGVIIDQYIVPK-DLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDIFEKI 124
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVFLEGaGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 125 QTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPI--MFFVtkkLV 202
Cdd:cd18584 81 LALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLipLFMI---LI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1267510758 203 AYSGKNFAKRQ-KDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVS 256
Cdd:cd18584 158 GKAAQAASRRQwAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRR 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
360-581 |
8.59e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 85.16 E-value: 8.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENV--SFGyeeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINslRGKIG 437
Cdd:PRK11432 7 VVLKNItkRFG---SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 438 VVLQDTYLFAG-TIMDNIRYG--RLDASDEEVINAAKAASAHSFIKHLPNQYETKIasegsnlSQGQKQLLAIARAILAD 514
Cdd:PRK11432 82 MVFQSYALFPHmSLGENVGYGlkMLGVPKEERKQRVKEALELVDLAGFEDRYVDQI-------SGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 515 ADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAH-RLKTIEKADQILVIKDGSIIEKGNHESL 581
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
360-569 |
9.14e-18 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 81.05 E-value: 9.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNikeydiNSLrgkigVV 439
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE------DLL-----FL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQDTYLFAGTIMDNIRYgrldASDEEvinaakaasahsfikhlpnqyetkiasegsnLSQGQKQLLAIARAILADADILI 519
Cdd:cd03223 70 PQRPYLPLGTLREQLIY----PWDDV-------------------------------LSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1267510758 520 LDEATSNIDTRTELQIQEGLNNLMrgrTSFV-IAHRlKTIEK-ADQILVIKD 569
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKELG---ITVIsVGHR-PSLWKfHDRVLDLDG 162
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
376-570 |
9.22e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.62 E-value: 9.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGkniKEYDINS----LRGKIGVVLQDTYLFAG-TI 450
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSprdaIALGIGMVHQHFMLVPNlTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 451 MDNIRYGrLDASDEEVINAAKAASAhsfIKHLPNQY------ETKIasegSNLSQGQKQLLAIARAILADADILILDEAT 524
Cdd:COG3845 98 AENIVLG-LEPTKGGRLDRKAARAR---IRELSERYgldvdpDAKV----EDLSVGEQQRVEILKALYRGARILILDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1267510758 525 SNIdtrTELQIQEgLNNLMR-----GRTSFVIAHRLKTI-EKADQILVIKDG 570
Cdd:COG3845 170 AVL---TPQEADE-LFEILRrlaaeGKSIIFITHKLREVmAIADRVTVLRRG 217
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
360-583 |
1.03e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.09 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSlRGKIGVV 439
Cdd:PRK13537 8 IDFRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQ-DTYLFAGTIMDNIR-YGRLdasdeeviNAAKAASAHSFIKHLPN--QYETKIASEGSNLSQGQKQLLAIARAILADA 515
Cdd:PRK13537 86 PQfDNLDPDFTVRENLLvFGRY--------FGLSAAAARALVPPLLEfaKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 516 DILILDEATSNIDTRTELQIQEGLNNLM-RGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESLME 583
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
47-317 |
1.28e-17 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 83.70 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 47 IFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTarMCLLLIAIYGVT----VFLTWLQIFVMVNVALKTIQKIRQDIFE 122
Cdd:cd18582 2 LLLLVLAKLLNVAVPFLLKYAVDALSAPASALLA--VPLLLLLAYGLArilsSLFNELRDALFARVSQRAVRRLALRVFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 123 KIQTLSLRFFDVRSQGDL---MSRVTNDIDNLnqaLTQSVVQIISSALTFIGVTIAMFAL-DWILAIVTLITVPIMFFVT 198
Cdd:cd18582 80 HLHSLSLRFHLSRKTGALsraIERGTRGIEFL---LRFLLFNILPTILELLLVCGILWYLyGWSYALITLVTVALYVAFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 199 KKLVAYSGKnFAKRQKDL-GELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNL 277
Cdd:cd18582 157 IKVTEWRTK-FRREMNEAdNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALIISL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1267510758 278 GMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQF 317
Cdd:cd18582 236 GLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFL 275
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
363-577 |
1.40e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 83.21 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 363 ENVSFGYEEN-----KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIK-EYDINSLRGKI 436
Cdd:PRK13633 8 KNVSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdEENLWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 437 GVVLQ--DTYLFAGTIMDNIRYG--RLDASDEE----VINAAKAASAHSFIKHLPNQyetkiasegsnLSQGQKQLLAIA 508
Cdd:PRK13633 88 GMVFQnpDNQIVATIVEEDVAFGpeNLGIPPEEirerVDESLKKVGMYEYRRHAPHL-----------LSGGQKQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267510758 509 RAILADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTIEKADQILVIKDGSIIEKGN 577
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
360-587 |
1.61e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 83.26 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKTI----LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI----KEYDINS 431
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegraLFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 432 LRGKIGVVLQ--DTYLFAGTIMDNIRYG--RLDASDEEVINAAKAASAHSFIKhlpnqyETKIASEGSNLSQGQKQLLAI 507
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGpqNFGVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 508 ArAILA-DADILILDEATSNIDTRTELQIQEGLNNLMR-GRTSFVIAHRLKTI-EKADQILVIKDGSIIEKGNHESLMED 584
Cdd:PRK13649 157 A-GILAmEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKPKDIFQD 235
|
...
gi 1267510758 585 RGF 587
Cdd:PRK13649 236 VDF 238
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
360-584 |
2.80e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.11 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKTI-LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGV 438
Cdd:PRK13648 8 IVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 439 VLQD-TYLFAGTIMD-NIRYGRLDasdeeviNAAKAASAHSFIKHLPNQYE--TKIASEGSNLSQGQKQLLAIARAILAD 514
Cdd:PRK13648 88 VFQNpDNQFVGSIVKyDVAFGLEN-------HAVPYDEMHRRVSEALKQVDmlERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267510758 515 ADILILDEATSNIDTRTELQIQEGLNNLMRGR--TSFVIAHRLKTIEKADQILVIKDGSIIEKGNHESLMED 584
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
365-582 |
3.10e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.12 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 365 VSFGyeeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVLQDTY 444
Cdd:PRK09536 11 VEFG---DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 445 L-FAGTIMDNIRYGRL----------DASDEEVINAAKAASAHSFikhlpnqyetkIASEGSNLSQGQKQLLAIARAILA 513
Cdd:PRK09536 88 LsFEFDVRQVVEMGRTphrsrfdtwtETDRAAVERAMERTGVAQF-----------ADRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267510758 514 DADILILDEATSNIDTRTELQIQEGLNNLMR-GRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESLM 582
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLVDdGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
372-546 |
3.38e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.30 E-value: 3.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 372 NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIkeyDINSLRGKIgvvlqdTYLfaG--- 448
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEAC------HYL--Ghrn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 449 ------TIMDNIRY-GRLDASDEEVINAAKAASAHSFIKHLPNQYetkiasegsnLSQGQKQLLAIARAILADADILILD 521
Cdd:PRK13539 83 amkpalTVAENLEFwAAFLGGEELDIAAALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILD 152
|
170 180
....*....|....*....|....*
gi 1267510758 522 EATSNIDTRTelqiQEGLNNLMRGR 546
Cdd:PRK13539 153 EPTAALDAAA----VALFAELIRAH 173
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
378-584 |
4.71e-17 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 82.84 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 378 EVSLKARPGETIALVGPTGSGKTTIINL---LTRFydiQQGQIHIDGK---------NIKEYdinslRGKIGVVLQDTYL 445
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLERP---DSGRIRLGGEvlqdsargiFLPPH-----RRRIGYVFQEARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 446 FAG-TIMDNIRYGRLdasdeeviNAAKAASAHSF--------IKHLPNQYETkiasegsNLSQGQKQLLAIARAILADAD 516
Cdd:COG4148 89 FPHlSVRGNLLYGRK--------RAPRAERRISFdevvellgIGHLLDRRPA-------TLSGGERQRVAIGRALLSSPR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267510758 517 ILILDEATSNIDTRTELQIQEGLNNLmrgRTSFVI-----AHRLKTIEK-ADQILVIKDGSIIEKGNHESLMED 584
Cdd:COG4148 154 LLLMDEPLAALDLARKAEILPYLERL---RDELDIpilyvSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
376-584 |
5.78e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.16 E-value: 5.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSL----RGKIGVVLQDTYLFAG-TI 450
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 451 MDNIRYGRLDAS------DEEVINAAKAASAHSFIKHLPNQyetkiasegsnLSQGQKQLLAIARAILADADILILDEAT 524
Cdd:PRK10070 124 LDNTAFGMELAGinaeerREKALDALRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267510758 525 SNIDTRTELQIQEGLNNLM--RGRTSFVIAHRL-KTIEKADQILVIKDGSIIEKGNHESLMED 584
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
360-584 |
6.95e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 81.36 E-value: 6.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEE----NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI----KEYDINS 431
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 432 LRGKIGVVLQ--DTYLFAGTIMDNIRYG--RLDASDEEVinaakAASAHSFIKHLpnQYETKIASEGS-NLSQGQKQLLA 506
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGpkNFKMNLDEV-----KNYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 507 IARAILADADILILDEATSNIDTRTELQIQEGLNNLM--RGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESLME 583
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFK 235
|
.
gi 1267510758 584 D 584
Cdd:PRK13646 236 D 236
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
360-582 |
8.02e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.01 E-value: 8.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKTilkEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNikEYDINSLRGKIGVV 439
Cdd:PRK10771 2 LKLTDITWLYHHLPM---RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD--HTTTPPSRRPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQDTYLFAG-TIMDNIRYG-----RLDASDEEVINA-AKAASAHSFIKHLPNQyetkiasegsnLSQGQKQLLAIARAIL 512
Cdd:PRK10771 77 FQENNLFSHlTVAQNIGLGlnpglKLNAAQREKLHAiARQMGIEDLLARLPGQ-----------LSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 513 ADADILILDEATSNIDT--RTEL-----QI--QEGLNNLMrgrtsfvIAHRLktiEKADQI----LVIKDGSIIEKGNHE 579
Cdd:PRK10771 146 REQPILLLDEPFSALDPalRQEMltlvsQVcqERQLTLLM-------VSHSL---EDAARIaprsLVVADGRIAWDGPTD 215
|
...
gi 1267510758 580 SLM 582
Cdd:PRK10771 216 ELL 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
339-588 |
1.79e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 80.66 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 339 DEVPEIKNKKDAFVVQNLQGHVALENVSFGYEENKTILkevslkarpgetiaLVGPTGSGKTTIIN-----LLTRFYDIQ 413
Cdd:PRK13631 19 DIILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYF--------------IIGNSGSGKSTLVThfnglIKSKYGTIQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 414 QGQIHIDGKNIKEYDINS-----------LRGKIGVVLQ--DTYLFAGTIMDNIRYGRLdASDEEVINAAKAASAHSFIK 480
Cdd:PRK13631 85 VGDIYIGDKKNNHELITNpyskkiknfkeLRRRVSMVFQfpEYQLFKDTIEKDIMFGPV-ALGVKKSEAKKLAKFYLNKM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 481 HLPNQYETKIASEgsnLSQGQKQLLAIArAILA-DADILILDEATSNIDTRTELQIQEG-LNNLMRGRTSFVIAHRL-KT 557
Cdd:PRK13631 164 GLDDSYLERSPFG---LSGGQKRRVAIA-GILAiQPEILIFDEPTAGLDPKGEHEMMQLiLDAKANNKTVFVITHTMeHV 239
|
250 260 270
....*....|....*....|....*....|.
gi 1267510758 558 IEKADQILVIKDGSIIEKGNHESLMEDRGFY 588
Cdd:PRK13631 240 LEVADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
371-576 |
1.88e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 77.95 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 371 ENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRF--YDIQQGQIHIDGKNIKEYDIN--SLRGkIGVVLQDTYLF 446
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEerARLG-IFLAFQYPPEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 447 AG-TIMDNIRYgrldasdeevINaakaasahsfikhlpnqyetkiasEGsnLSQGQKQLLAIARAILADADILILDEATS 525
Cdd:cd03217 90 PGvKNADFLRY----------VN------------------------EG--FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1267510758 526 NIDTRTELQIQEGLNNLMRGRTSF-VIAHRLKTIE--KADQILVIKDGSIIEKG 576
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEGKSVlIITHYQRLLDyiKPDRVHVLYDGRIVKSG 187
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
353-576 |
2.03e-16 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 82.42 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 353 VQNLqghvaleNVSFG-YEENKTILKEVSLKARPGETIALVGPTGSGKT----TIINLLTRFYDIQQGQIHIDGKNI--- 424
Cdd:COG4172 9 VEDL-------SVAFGqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLlgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 425 KEYDINSLRG-KIGVVLQD--TYL---FagTIMDNIRygrldasdeEVI---NAAKAASAHSFIKHL------PNQyETK 489
Cdd:COG4172 82 SERELRRIRGnRIAMIFQEpmTSLnplH--TIGKQIA---------EVLrlhRGLSGAAARARALELlervgiPDP-ERR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 490 IASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTIEK-ADQILV 566
Cdd:COG4172 150 LDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRelGMALLLITHDLGVVRRfADRVAV 229
|
250
....*....|
gi 1267510758 567 IKDGSIIEKG 576
Cdd:COG4172 230 MRQGEIVEQG 239
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
362-585 |
2.73e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.51 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIkEYD---INSLRGKIGV 438
Cdd:PRK13636 8 VEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSrkgLMKLRESVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 439 VLQ--DTYLFAGTIMDNIRYGRLDAS--DEEVINAAKAASAHSFIKHLPNQyetkiasEGSNLSQGQKQLLAIARAILAD 514
Cdd:PRK13636 87 VFQdpDNQLFSASVYQDVSFGAVNLKlpEDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267510758 515 ADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTIE-KADQILVIKDGSIIEKGNHESLMEDR 585
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
379-584 |
2.98e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 80.01 E-value: 2.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 379 VSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYD---INSLRGKIGVVLQDTYlfaGTImdNIR 455
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNPY---GSL--NPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 456 YgRLDASDEE--VIN-----AAKAASAHSFIKHL---PNQYEtkiaSEGSNLSQGQKQLLAIARAILADADILILDEATS 525
Cdd:PRK11308 109 K-KVGQILEEplLINtslsaAERREKALAMMAKVglrPEHYD----RYPHMFSGGQRQRIAIARALMLDPDVVVADEPVS 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267510758 526 NIDTRTELQIqegLNNLM----RGRTSFV-IAHRLKTIEK-ADQILVIKDGSIIEKGNHESLMED 584
Cdd:PRK11308 184 ALDVSVQAQV---LNLMMdlqqELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
376-581 |
3.05e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.88 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGK-----NIKEydinSLRGKIGVVLQDTYLFAG-T 449
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfaSTTA----ALAAGVAIIYQELHLVPEmT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 450 IMDNIRYGRLDASDEEVINAAKAASAHSFIKHL-----PNqyeTKIASegsnLSQGQKQLLAIARAILADADILILDEAT 524
Cdd:PRK11288 96 VAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLgvdidPD---TPLKY----LSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 525 SNIDTRtELQIQEGLNNLMR--GRTSFVIAHRLKTI-EKADQILVIKDGSIIEkgNHESL 581
Cdd:PRK11288 169 SSLSAR-EIEQLFRVIRELRaeGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDM 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
362-570 |
5.65e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 75.18 E-value: 5.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNikeydinslrgKIGVVLQ 441
Cdd:cd03221 3 LENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------KIGYFEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 442 dtylfagtimdnirygrldasdeevinaakaasahsfikhlpnqyetkiasegsnLSQGQKQLLAIARAILADADILILD 521
Cdd:cd03221 71 -------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1267510758 522 EATSNIDTRTELQIQEGLNNLmrGRTSFVIAH-R--LKTIekADQILVIKDG 570
Cdd:cd03221 96 EPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQV--ATKIIELEDG 143
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
376-576 |
6.09e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.98 E-value: 6.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDIN-SLRGKIGVVLQDTYLFAG-TIMDN 453
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 454 IRYGRLDASDEEVINAA------KAASAHSFIKHLPNQYETKIAsegsNLSQGQKQLLAIARAILADADILILDEATSNI 527
Cdd:PRK09700 101 LYIGRHLTKKVCGVNIIdwremrVRAAMMLLRVGLKVDLDEKVA----NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1267510758 528 dTRTELQIQEGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKG 576
Cdd:PRK09700 177 -TNKEVDYLFLIMNQLRkeGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
362-573 |
6.53e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 81.31 E-value: 6.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGY---EENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSL----RG 434
Cdd:PRK10535 7 LKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 435 KIGVVLQDTYLFAG-TIMDNIRYGRLDASDEEvinAAKAASAHSFIKHLpnQYETKIASEGSNLSQGQKQLLAIARAILA 513
Cdd:PRK10535 87 HFGFIFQRYHLLSHlTAAQNVEVPAVYAGLER---KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267510758 514 DADILILDEATSNIDTRTELQIQEGLNNLM-RGRTSFVIAHRLKTIEKADQILVIKDGSII 573
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
323-584 |
7.98e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.67 E-value: 7.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 323 TIQAAVAGGERVFEIMDEVPEIKNKKDAFVVQNLQGHvALENVSFgyeenktilkevslKARPGETIALVGPTGSGKTTI 402
Cdd:PRK10261 302 IEQDTVVDGEPILQVRNLVTRFPLRSGLLNRVTREVH-AVEKVSF--------------DLWPGETLSLVGESGSGKSTT 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 403 INLLTRFYDIQQGQIHIDGKNI---KEYDINSLRGKIGVVLQDTY-------LFAGTIMDNIRYGRLDASDEEvinAAKA 472
Cdd:PRK10261 367 GRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPYasldprqTVGDSIMEPLRVHGLLPGKAA---AARV 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 473 ASAHSFIKHLPnQYETKIASEgsnLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFV 550
Cdd:PRK10261 444 AWLLERVGLLP-EHAWRYPHE---FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLF 519
|
250 260 270
....*....|....*....|....*....|....*
gi 1267510758 551 IAHRLKTIEK-ADQILVIKDGSIIEKGNHESLMED 584
Cdd:PRK10261 520 ISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFEN 554
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
357-576 |
8.31e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 76.93 E-value: 8.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 357 QGHVALENVSFGY-EENKT--ILKEVSLKARPGETIALVGPTGSGKTTIINLLT---RFYDIQQGQIHIDGKNIKEYdin 430
Cdd:cd03234 1 QRVLPWWDVGLKAkNWNKYarILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPRKPD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 431 SLRGKIGVVLQDTYLFAG-TIMDNIRYGRLDASDEEVINAAKAASAHSF-IKHLPNqyeTKIASEG-SNLSQGQKQLLAI 507
Cdd:cd03234 78 QFQKCVAYVRQDDILLPGlTVRETLTYTAILRLPRKSSDAIRKKRVEDVlLRDLAL---TRIGGNLvKGISGGERRRVSI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267510758 508 ARAILADADILILDEATSNIDTRTELQIQEGLNNLMRgRTSFVIAhrlkTIEKA--------DQILVIKDGSIIEKG 576
Cdd:cd03234 155 AVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLAR-RNRIVIL----TIHQPrsdlfrlfDRILLLSSGEIVYSG 226
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
46-334 |
1.21e-15 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 77.57 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 46 VIFLVFVTTLLGLLGPYLMGVIIDQYIvpkdlSGTARMCLLLIAIYGVTVFL----------TWLQIFVMvNVALKTIQK 115
Cdd:cd18583 1 CFLCLLAERVLNVLVPRQLGIIVDSLS-----GGSGKSPWKEIGLYVLLRFLqsggglgllrSWLWIPVE-QYSYRALST 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 116 IrqdIFEKIQTLSLRFFDVRSQGDLMSrvtndidNLNQAltQSVVQIISSAL-----TFIGVTIAM----FALDWILAIV 186
Cdd:cd18583 75 A---AFNHVMNLSMDFHDSKKSGEVLK-------AIEQG--SSINDLLEQILfqivpMIIDLVIAIvylyYLFDPYMGLI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 187 TLITVPIMFFVTKKLVAYSgknfAKRQKDLgeLNGFIEEAITGADVTTLYgkekETVQNFNKIN-EQLRVSAT-----KA 260
Cdd:cd18583 143 VAVVMVLYVWSTIKLTSWR----TKLRRDM--IDADREERSILTESLLNW----ETVKYFNREPyEKERYREAvknyqKA 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 261 DTFSAFIFPSMNFINNLGM--GLVIGT--GSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18583 213 ERKYLFSLNLLNAVQSLILtlGLLAGCflAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
46-329 |
1.37e-15 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 77.71 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 46 VIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDIFEKIQ 125
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 126 TLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTKKLVAYS 205
Cdd:cd18561 81 KLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 206 GKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLVIGT 285
Cdd:cd18561 161 KDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1267510758 286 GSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVA 329
Cdd:cd18561 241 GALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGIS 284
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
375-582 |
1.80e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 76.55 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 375 ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIK-------------EYDINSLRGKIGVVLQ 441
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 442 DTYLFAG-TIMDNIRYGRLdasdeEVINAAKAASAHSFIKHLpNQYETKIASEG---SNLSQGQKQLLAIARAILADADI 517
Cdd:PRK10619 100 HFNLWSHmTVLENVMEAPI-----QVLGLSKQEARERAVKYL-AKVGIDERAQGkypVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267510758 518 LILDEATSNIDTRTELQIQEGLNNLM-RGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESLM 582
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
61-334 |
2.18e-15 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 77.13 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 61 PYLMGVIIDqYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQ-KIRQDIFEKIQTLSLRFFDVRSQGD 139
Cdd:cd18589 16 PYYTGRMTD-WIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHsRLQGLVFAAVLRQEIAFFDSNQTGD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 140 LMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTKKLVAYSgKNFAKR-QKDLGE 218
Cdd:cd18589 95 IVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQ-QSLAVQvQKSLAR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 219 LNGFIEEAITG-ADVTTLYGKEKET------VQNFNKINeQLRVSATKADTFSAfifpSMNfinnlGMGLVIGT---GSV 288
Cdd:cd18589 174 ANQVAVETFSAmKTVRSFANEEGEAqryrqrLQKTYRLN-KKEAAAYAVSMWTS----SFS-----GLALKVGIlyyGGQ 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1267510758 289 MVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18589 244 LVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
373-576 |
2.99e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.94 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 373 KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTrFYDIQ----QGQIHIDGKNIkeyDINSLRGKIGVVLQDTyLFAG 448
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPI---DAKEMRAISAYVQQDD-LFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 449 T--------IMDNIRYGRLDASDE------EVINAAKAASAHsfikhlpnqyETKIASEGS--NLSQGQKQLLAIARAIL 512
Cdd:TIGR00955 113 TltvrehlmFQAHLRMPRRVTKKEkrervdEVLQALGLRKCA----------NTRIGVPGRvkGLSGGERKRLAFASELL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267510758 513 ADADILILDEATSNIDTRTELQIQEGLNNL-MRGRTSFVIAHR--LKTIEKADQILVIKDGSIIEKG 576
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQpsSELFELFDKIILMAEGRVAYLG 249
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
360-576 |
3.19e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 77.38 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDiNSLRGkIGVV 439
Cdd:PRK11000 4 VTLRNVTKAYGDV-VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVP-PAERG-VGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQDTYLFAG-TIMDNIRYG-RLDASDEEVINaaKAASAHSFIKHLPNQYETKIASegsnLSQGQKQLLAIARAILADADI 517
Cdd:PRK11000 81 FQSYALYPHlSVAENMSFGlKLAGAKKEEIN--QRVNQVAEVLQLAHLLDRKPKA----LSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267510758 518 LILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAH-RLKTIEKADQILVIKDGSIIEKG 576
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
363-584 |
4.66e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.93 E-value: 4.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 363 ENVSFGYEENKtILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDIN--SLRGkIGVVL 440
Cdd:PRK10895 7 KNLAKAYKGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHarARRG-IGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 441 QDTYLFAG-TIMDNIRYG---RLDASDEEVINAAKAASAHSFIKHLPNqyetkiaSEGSNLSQGQKQLLAIARAILADAD 516
Cdd:PRK10895 85 QEASIFRRlSVYDNLMAVlqiRDDLSAEQREDRANELMEEFHIEHLRD-------SMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 517 ILILDEATSNIDTRTELQIQEGLNNLM-RGRTSFVIAHRLK-TIEKADQILVIKDGSIIEKGNHESLMED 584
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVReTLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
376-585 |
5.14e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.74 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDI-NSLRGKIGVVLQDTYLFAG-TIMDN 453
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPkSSQEAGIGIIHQELNLIPQlTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 454 IRYGRLDASDEEVINAAKA-ASAHSFIKHLPNQYETKIASegSNLSQGQKQLLAIARAILADADILILDEATSNI-DTRT 531
Cdd:PRK10762 100 IFLGREFVNRFGRIDWKKMyAEADKLLARLNLRFSSDKLV--GELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTET 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 532 elqiqEGLNNLMR-----GRTSFVIAHRLKTI-EKADQILVIKDGSIIEKGNHESLMEDR 585
Cdd:PRK10762 178 -----ESLFRVIRelksqGRGIVYISHRLKEIfEICDDVTVFRDGQFIAEREVADLTEDS 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
363-581 |
1.03e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 74.84 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 363 ENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVLQ- 441
Cdd:PRK13652 7 RDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 442 -DTYLFAGTIMDNIRYGRLDAS-DEEVINAAKAASAHSF-IKHLPNQYEtkiasegSNLSQGQKQLLAIARAILADADIL 518
Cdd:PRK13652 87 pDDQIFSPTVEQDIAFGPINLGlDEETVAHRVSSALHMLgLEELRDRVP-------HHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267510758 519 ILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTI-EKADQILVIKDGSIIEKGNHESL 581
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
61-306 |
1.09e-14 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 74.65 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 61 PYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQI-FVMVNVALKTIqKIRQDIFEKIQTLSLRFFDVRSQGD 139
Cdd:cd18784 16 PYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGgLFTLAMARLNI-RIRNLLFRSIVSQEIGFFDTVKTGD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 140 LMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTKKLVAYSGKNFAKRQKDLGEL 219
Cdd:cd18784 95 ITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 220 NGFIEEAITGAdvttlygkekETVQNF-NKINEQLRVSATKADTFS-----AFIFPSMNFINNL-GMGLVIGT---GSVM 289
Cdd:cd18784 175 NEVAEETISSI----------RTVRSFaNEDGEANRYSEKLKDTYKlkikeALAYGGYVWSNELtELALTVSTlyyGGHL 244
|
250
....*....|....*..
gi 1267510758 290 VLNGMTTVGVIAAFINY 306
Cdd:cd18784 245 VITGQISGGNLISFILY 261
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
374-585 |
1.35e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 76.40 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 374 TILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFY--DIQQGQIHIDGKNIKEYDI-NSLRGKIGVVLQDTYLFAG-T 449
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIrDTERAGIVIIHQELTLVPElS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 450 IMDNIRYG--------RLDasDEEVINAAKAASAHSFIKHLPNqyetkiASEGSNLSQGQKQLLAIARAILADADILILD 521
Cdd:TIGR02633 95 VAENIFLGneitlpggRMA--YNAMYLRAKNLLRELQLDADNV------TRPVGDYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 522 EATSNIdTRTELQIqegLNNLMR-----GRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESLMEDR 585
Cdd:TIGR02633 167 EPSSSL-TEKETEI---LLDIIRdlkahGVACVYISHKLNEVKAvCDTICVIRDGQHVATKDMSTMSEDD 232
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
372-587 |
2.62e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 73.14 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 372 NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRF--YDIQQGQIHIDGKNIKEYDiNSLRGKIGVVLQDTYLFAGT 449
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLE-PEERAHLGIFLAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 450 IMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYE---------TKIASEGsnLSQGQKQLLAIARAILADADILIL 520
Cdd:CHL00131 98 GVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKlvgmdpsflSRNVNEG--FSGGEKKRNEILQMALLDSELAIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267510758 521 DEATSNIDTRTELQIQEGLNNLMRGRTSFV-IAH--RLKTIEKADQILVIKDGSIIEKGNHE--SLMEDRGF 587
Cdd:CHL00131 176 DETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElaKELEKKGY 247
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
376-584 |
4.50e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 72.56 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDInSLRGK-IGVVLQDtylfAGTIMD-N 453
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDY-KYRCKhIRMIFQD----PNTSLNpR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 454 IRYGR-LDA--------SDEEvinaakaasAHSFIKH-------LPNQYETKIasegSNLSQGQKQLLAIARAILADADI 517
Cdd:COG4167 104 LNIGQiLEEplrlntdlTAEE---------REERIFAtlrlvglLPEHANFYP----HMLSSGQKQRVALARALILQPKI 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 518 LILDEATSNID--TRT-------ELQIQEGLnnlmrgrtSFV-IAHRLKTIEK-ADQILVIKDGSIIEKGNHESLMED 584
Cdd:COG4167 171 IIADEALAALDmsVRSqiinlmlELQEKLGI--------SYIyVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
366-531 |
8.45e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.76 E-value: 8.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 366 SFGYEEN---KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDgknIKEYDINSLRgkigvvlqd 442
Cdd:COG2401 33 AFGVELRvveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD---VPDNQFGREA--------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 443 tylfagTIMDNIryGRLDASDE--EVINAAKAASAHSFIKHLpnqyetkiasegSNLSQGQKQLLAIARAILADADILIL 520
Cdd:COG2401 101 ------SLIDAI--GRKGDFKDavELLNAVGLSDAVLWLRRF------------KELSTGQKFRFRLALLLAERPKLLVI 160
|
170
....*....|.
gi 1267510758 521 DEATSNIDTRT 531
Cdd:COG2401 161 DEFCSHLDRQT 171
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
328-576 |
8.72e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 71.21 E-value: 8.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 328 VAGGERVFEIMDEVPEIKNKKDAFVVQNLQGHVALENVSFGYEEnktilkevslkarpGETIALVGPTGSGKTTIINLLT 407
Cdd:cd03267 3 VSNLSKSYRVYSKEPGLIGSLKSLFKRKYREVEALKGISFTIEK--------------GEIVGFIGPNGAGKTTTLKILS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 408 RFYDIQQGQIHIDGkNIKEYDINSLRGKIGVVL------------QDTYLFAGTIMDnIRYGRLDASDEEVINAAKaasa 475
Cdd:cd03267 69 GLLQPTSGEVRVAG-LVPWKRRKKFLRRIGVVFgqktqlwwdlpvIDSFYLLAAIYD-LPPARFKKRLDELSELLD---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 476 hsfIKHLPNQyetkiasEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVI--AH 553
Cdd:cd03267 143 ---LEELLDT-------PVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLltSH 212
|
250 260
....*....|....*....|....
gi 1267510758 554 RLKTIEK-ADQILVIKDGSIIEKG 576
Cdd:cd03267 213 YMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
360-581 |
9.28e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 71.27 E-value: 9.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFgyEENKTILKEVSLKARPGETIALVGPTGSGKT----TIINLLTRFYDIQQGQIHIDGKnikEYDINSLRGK 435
Cdd:PRK10418 5 IELRNIAL--QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGK---PVAPCALRGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 436 IgvvlqdtylfAGTIMDNIR-------------------YGRL--DASDEEVINAAKAASAHSFIKHLPNQyetkiaseg 494
Cdd:PRK10418 80 K----------IATIMQNPRsafnplhtmhtharetclaLGKPadDATLTAALEAVGLENAARVLKLYPFE--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 495 snLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTS--FVIAHRLKTIEK-ADQILVIKDGS 571
Cdd:PRK10418 141 --MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVARlADDVAVMSHGR 218
|
250
....*....|
gi 1267510758 572 IIEKGNHESL 581
Cdd:PRK10418 219 IVEQGDVETL 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
360-570 |
1.14e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 70.67 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI---KEYDINSLRGKI 436
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 437 GVVLQDTYLFAG-TIMDNIRYGRL--DASDEEVINAAKAASAHSFI----KHLPNQyetkiasegsnLSQGQKQLLAIAR 509
Cdd:PRK10908 82 GMIFQDHHLLMDrTVYDNVAIPLIiaGASGDDIRRRVSAALDKVGLldkaKNFPIQ-----------LSGGEQQRVGIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267510758 510 AILADADILILDEATSNID---TRTELQIQEGLNNLmrGRTSFVIAHRLKTIEKAD-QILVIKDG 570
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRV--GVTVLMATHDIGLISRRSyRMLTLSDG 213
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
360-586 |
1.17e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.68 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKTiLKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINS-LRGKIGV 438
Cdd:PRK11614 6 LSFDKVSAHYGKIQA-LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 439 VLQDTYLFAG-TIMDNIRYGRLDASDEEVINAAKAASAhsfikHLPNQYETKIASEGSnLSQGQKQLLAIARAILADADI 517
Cdd:PRK11614 85 VPEGRRVFSRmTVEENLAMGGFFAERDQFQERIKWVYE-----LFPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267510758 518 LILDEATSNIDTRTELQIQEGLNNLM-RGRTSFVIAhrlktiEKADQILVIKD-GSIIEKGNheSLMEDRG 586
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLReQGMTIFLVE------QNANQALKLADrGYVLENGH--VVLEDTG 221
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
361-565 |
1.69e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.13 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 361 ALENVSFGYEENKtILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVL 440
Cdd:PRK10247 9 QLQNVGYLAGDAK-ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 441 QDTYLFAGTIMDNIRYG---RLDASDEEVInaakAASAHSFikHLPNQYETKIASEgsnLSQGQKQLLAIARAILADADI 517
Cdd:PRK10247 88 QTPTLFGDTVYDNLIFPwqiRNQQPDPAIF----LDDLERF--ALPDTILTKNIAE---LSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1267510758 518 LILDEATSNIDTRTELQIQEGLNNLMRGRTSFVI--AHRLKTIEKADQIL 565
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINHADKVI 208
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
357-580 |
1.81e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.07 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 357 QGHVALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKI 436
Cdd:PRK15056 4 QAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 437 GVVLQDTYLFAGTIMDNI---RYG------RLDASDEEVINAAKAASAHSFIKHlpnqyetkiaSEGSNLSQGQKQLLAI 507
Cdd:PRK15056 84 PQSEEVDWSFPVLVEDVVmmgRYGhmgwlrRAKKRDRQIVTAALARVDMVEFRH----------RQIGELSGGQKKRVFL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267510758 508 ARAILADADILILDEATSNIDTRTELQIQEGLNNLM-RGRTSFVIAHRLKTI-EKADQILVIKdGSIIEKGNHES 580
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVtEFCDYTVMVK-GTVLASGPTET 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
376-574 |
1.84e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.90 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDI--QQGQIHIDGKNIKEYDINSLRgKIGVVL--QD----TYLfa 447
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDGEVCRFKDIRDSE-ALGIVIihQElaliPYL-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 448 gTIMDNI-------RYGRLDAsdEEVINAAKAASAHSFIKHLPnqyETKIasegSNLSQGQKQLLAIARAILADADILIL 520
Cdd:NF040905 94 -SIAENIflgneraKRGVIDW--NETNRRARELLAKVGLDESP---DTLV----TDIGVGKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 521 DEATSNI---DTRTELQIQEGLNNlmRGRTSFVIAHRLKTIEK-ADQILVIKDGSIIE 574
Cdd:NF040905 164 DEPTAALneeDSAALLDLLLELKA--QGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
371-587 |
2.36e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 70.21 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 371 ENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLT--RFYDIQQGQIHIDGKNIKEYDINSLRGKiGVVLQDTY---- 444
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAGE-GIFMAFQYpvei 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 445 ------LFAGTIMDNIRYGR----LDASDEEVINAAKAAsahsfIKHLPNQYETKIASEGsnLSQGQKQLLAIARAILAD 514
Cdd:PRK09580 91 pgvsnqFFLQTALNAVRSYRgqepLDRFDFQDLMEEKIA-----LLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 515 ADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIA---HRLKTIEKADQILVIKDGSIIEKGNHESL--MEDRGF 587
Cdd:PRK09580 164 PELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVthyQRILDYIKPDYVHVLYQGRIVKSGDFTLVkqLEEQGY 241
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
356-594 |
3.19e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.04 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 356 LQGHVALENVSFGYEENKTiLKEVSLKARPGETIALVGPTGSGKTTIINLLTRFY---DIQQGQIHIDGKNIKE-----Y 427
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQA-LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQRegrlaR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 428 DINSLRGKIGVVLQDTYLFAG-TIMDNIRYGRLDAS----------DEEVINAAKAASAHSFIKHLPNQyetkiasEGSN 496
Cdd:PRK09984 80 DIRKSRANTGYIFQQFNLVNRlSVLENVLIGALGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQ-------RVST 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 497 LSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLK-TIEKADQILVIKDGSII 573
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVF 232
|
250 260
....*....|....*....|..
gi 1267510758 574 EKGNHESLMEDRgfyFD-LYTS 594
Cdd:PRK09984 233 YDGSSQQFDNER---FDhLYRS 251
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
376-570 |
3.93e-13 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 69.03 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLrgkigVVLQDTYLFAG-TIMDNI 454
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 455 rygrldasdeevinaakAASAHSFIKHLPNQYETKIASEG--------------SNLSQGQKQLLAIARAILADADILIL 520
Cdd:TIGR01184 76 -----------------ALAVDRVLPDLSKSERRAIVEEHialvglteaadkrpGQLSGGMKQRVAIARALSIRPKVLLL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1267510758 521 DEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRL-KTIEKADQILVIKDG 570
Cdd:TIGR01184 139 DEPFGALDALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
364-570 |
4.08e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.07 E-value: 4.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 364 NVSFGYEENKT---ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINS---LRG-KI 436
Cdd:PRK11629 10 NLCKRYQEGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNqKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 437 GVVLQDTYLFAG-TIMDNIRYGRLdasdeevINAAKAASAHSFIKHLPNQ--YETKIASEGSNLSQGQKQLLAIARAILA 513
Cdd:PRK11629 90 GFIYQFHHLLPDfTALENVAMPLL-------IGKKKPAEINSRALEMLAAvgLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1267510758 514 DADILILDEATSNIDTRTELQIQEGLNNL-MRGRTSF-VIAHRLKTIEKADQILVIKDG 570
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFlVVTHDLQLAKRMSRQLEMRDG 221
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
46-325 |
6.40e-13 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 69.53 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 46 VIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDIFEKIQ 125
Cdd:cd18566 7 VLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 126 TLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSaLTFIGVTIA-MFALDWILAIVTLITVPIMFFVTkklvAY 204
Cdd:cd18566 87 SLPLSFFEREPSGAHLERL-NSLEQIREFLTGQALLALLD-LPFVLIFLGlIWYLGGKLVLVPLVLLGLFVLVA----IL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 205 SGKNFAKRQKDLGELN----GFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMG 280
Cdd:cd18566 161 LGPILRRALKERSRADerrqNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1267510758 281 LVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQ 325
Cdd:cd18566 241 AVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQ 285
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
87-334 |
6.96e-13 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 69.50 E-value: 6.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 87 LIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSA 166
Cdd:cd18574 48 LLGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 167 LTFIGVTIAMFALDWILAIVTLITVPIMFFV----TKKLVAYSGKnfAKRQkdLGELNGFIEEAITgaDVTTL--YGKEK 240
Cdd:cd18574 128 TQTVGCVVSLYLISPKLTLLLLVIVPVVVLVgtlyGSFLRKLSRR--AQAQ--VAKATGVADEALG--NIRTVraFAMED 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 241 ETVQNFNKINEQLRVSATKADT----FSAFifpSMNFINNLGMGlVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQ 316
Cdd:cd18574 202 RELELYEEEVEKAAKLNEKLGLgigiFQGL---SNLALNGIVLG-VLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQ 277
|
250
....*....|....*...
gi 1267510758 317 FATLMNTIQAAVAGGERV 334
Cdd:cd18574 278 LSVLFGQYVKGKSAGARV 295
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
360-576 |
7.12e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 69.27 E-value: 7.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKtILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGK--NIKEYDINSLRGKIG 437
Cdd:PRK13638 2 LATSDLWFRYQDEP-VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 438 VVLQD--TYLFAGTIMDNIRYG--RLDASDEEVI----NAAKAASAHSFiKHLPNQYetkiasegsnLSQGQKQLLAIAR 509
Cdd:PRK13638 81 TVFQDpeQQIFYTDIDSDIAFSlrNLGVPEAEITrrvdEALTLVDAQHF-RHQPIQC----------LSHGQKKRVAIAG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267510758 510 AILADADILILDEATSNIDTRTELQIQEGLNNLM-RGRTSFVIAHRLKTI-EKADQILVIKDGSIIEKG 576
Cdd:PRK13638 150 ALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHG 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
350-572 |
7.39e-13 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 67.07 E-value: 7.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 350 AFVVQNLQGHVALENVSFgyeenktilkevslKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDI 429
Cdd:cd03215 4 VLEVRGLSVKGAVRDVSF--------------EVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 430 -NSLRGKIGVVLQD---TYLFAG-TIMDNIRYGRLdasdeevinaakaasahsfikhlpnqyetkiasegsnLSQGQKQL 504
Cdd:cd03215 70 rDAIRAGIAYVPEDrkrEGLVLDlSVAENIALSSL-------------------------------------LSGGNQQK 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 505 LAIARAILADADILILDEATSNIDTRTELQIQEGLNNL-MRGRTSFVIAHRLKTI-EKADQILVIKDGSI 572
Cdd:cd03215 113 VVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELaDAGKAVLLISSELDELlGLCDRILVMYEGRI 182
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
371-577 |
7.82e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.57 E-value: 7.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 371 ENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeydINSLrgkIGVvlqdtylfaGTI 450
Cdd:COG1134 37 EEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR------VSAL---LEL---------GAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 451 M-------DNIR-YGR-LDASDEEVinAAKAASAHSF----------IKHlpnqYetkiasegsnlSQGQKQLLAIARAI 511
Cdd:COG1134 99 FhpeltgrENIYlNGRlLGLSRKEI--DEKFDEIVEFaelgdfidqpVKT----Y-----------SSGMRARLAFAVAT 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 512 LADADILILDEATSNIDTRTELQIQEGLNNLM-RGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGN 577
Cdd:COG1134 162 AVDPDILLVDEVLAVGDAAFQKKCLARIRELReSGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
343-583 |
1.18e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 69.86 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 343 EIKNKKDAFvvqnlQGHVALENVSFgyeenkTILKevslkarpGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGK 422
Cdd:PRK11607 21 EIRNLTKSF-----DGQHAVDDVSL------TIYK--------GEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 423 NIKeyDINSLRGKIGVVLQDTYLFAG-TIMDNIRYG-RLDASDEEVINAAKA---ASAH--SFIKHLPNQyetkiasegs 495
Cdd:PRK11607 82 DLS--HVPPYQRPINMMFQSYALFPHmTVEQNIAFGlKQDKLPKAEIASRVNemlGLVHmqEFAKRKPHQ---------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 496 nLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQ-EGLNNLMR-GRTSFVIAH-RLKTIEKADQILVIKDGSI 572
Cdd:PRK11607 150 -LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQlEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKF 228
|
250
....*....|.
gi 1267510758 573 IEKGNHESLME 583
Cdd:PRK11607 229 VQIGEPEEIYE 239
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
379-576 |
1.54e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 67.71 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 379 VSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKeydinSLRG----KIGVV--LQDTYLFAG-TIM 451
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE-----GLPGhqiaRMGVVrtFQHVRLFREmTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 452 DNI--------------------RYGRldaSDEEVINAAKAASAHSFIKHLPNQyetkiasEGSNLSQGQKQLLAIARAI 511
Cdd:PRK11300 99 ENLlvaqhqqlktglfsgllktpAFRR---AESEALDRAATWLERVGLLEHANR-------QAGNLAYGQQRRLEIARCM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 512 LADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTI-EKADQILVIKDGSIIEKG 576
Cdd:PRK11300 169 VTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVmGISDRIYVVNQGTPLANG 236
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
43-199 |
2.84e-12 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 67.53 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 43 LTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQDIFE 122
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267510758 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVTK 199
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQR 157
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
360-565 |
3.16e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.68 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALEN--VSFGyeeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeydinsLRgkIG 437
Cdd:PRK09544 5 VSLENvsVSFG---QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 438 VVLQDTYLFAGTIMDNIRYGRL--DASDEEVINAAKAASAhsfiKHLPNQYETKiasegsnLSQGQKQLLAIARAILADA 515
Cdd:PRK09544 71 YVPQKLYLDTTLPLTVNRFLRLrpGTKKEDILPALKRVQA----GHLIDAPMQK-------LSGGETQRVLLARALLNRP 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1267510758 516 DILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTI-EKADQIL 565
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVmAKTDEVL 192
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
362-582 |
4.77e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.11 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGyeenkTILKEVSLKARPGETIALVGPTGSGKTTiinLLTRFYDI--QQGQIHIDGKNIKEYDINSL-RGKIGV 438
Cdd:PRK03695 3 LNDVAVS-----TRLGPLSAEVRAGEILHLVGPNGAGKST---LLARMAGLlpGSGSIQFAGQPLEAWSAAELaRHRAYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 439 VLQDTYLFAgtiMDNIRYgrLDASDEEVINAAKAASAHSFIKHLPnQYETKIASEGSNLSQGQKQ-------LLAIARAI 511
Cdd:PRK03695 75 SQQQTPPFA---MPVFQY--LTLHQPDKTRTEAVASALNEVAEAL-GLDDKLGRSVNQLSGGEWQrvrlaavVLQVWPDI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 512 LADADILILDEATSNIDTrtelqIQEG-LNNLMR-----GRTSFVIAHRL-KTIEKADQILVIKDGSIIEKGNHESLM 582
Cdd:PRK03695 149 NPAGQLLLLDEPMNSLDV-----AQQAaLDRLLSelcqqGIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
361-581 |
5.14e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.58 E-value: 5.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 361 ALENVSFGY---EENKTILKEVSLKARPGETIALVGPTGSGKT----TIINLL-TRFYDIQQGQIHIDGKNIKEYDINSL 432
Cdd:PRK15134 7 AIENLSVAFrqqQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGESLLHASEQTL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 433 RG----KIGVVLQDTyLFAGTIMDNI-----------RYGRLDASDEEVINAAKAASAHSFIKHL---PNQyetkiaseg 494
Cdd:PRK15134 87 RGvrgnKIAMIFQEP-MVSLNPLHTLekqlyevlslhRGMRREAARGEILNCLDRVGIRQAAKRLtdyPHQ--------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 495 snLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGS 571
Cdd:PRK15134 157 --LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGR 234
|
250
....*....|
gi 1267510758 572 IIEKGNHESL 581
Cdd:PRK15134 235 CVEQNRAATL 244
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
364-588 |
5.30e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.44 E-value: 5.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 364 NVSFGYEE-NKTILKEVSLKARPGETIALVGPTGSGKT----TIINLLTRFYDIQqGQIHIDGK---NIKEYDINSLRG- 434
Cdd:PRK09473 19 RVTFSTPDgDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIG-GSATFNGReilNLPEKELNKLRAe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 435 KIGVVLQDT------YLFAGT-----IMDNIRYGRLDASDEEV--INAAKAASAHSFIKHLPNQYetkiasegsnlSQGQ 501
Cdd:PRK09473 98 QISMIFQDPmtslnpYMRVGEqlmevLMLHKGMSKAEAFEESVrmLDAVKMPEARKRMKMYPHEF-----------SGGM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 502 KQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNH 578
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNA 246
|
250
....*....|
gi 1267510758 579 ESLmedrgFY 588
Cdd:PRK09473 247 RDV-----FY 251
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
387-591 |
5.75e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 69.27 E-value: 5.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 387 ETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIkEYDINSLRGKIGVVLQDTYLFAG-TIMDNIR-YGRLDA-SD 463
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILfYAQLKGrSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 464 EEVINAAKAASAHSFIKHLPNQyetkiasEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLM 543
Cdd:TIGR01257 1036 EEAQLEMEAMLEDTGLHHKRNE-------EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR 1108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1267510758 544 RGRTSFVIAHRLKTIE-KADQILVIKDGSIIEKGNHESLME--DRGFYFDL 591
Cdd:TIGR01257 1109 SGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPLFLKNcfGTGFYLTL 1159
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
385-580 |
6.36e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 67.21 E-value: 6.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 385 PGETI-ALVGPTGSGKTTIINL---LTRfydIQQGQIHIDGK--NIKEYDIN---SLRgKIGVVLQDTYLFAG-TIMDNI 454
Cdd:PRK11144 22 PAQGItAIFGRSGAGKTSLINAisgLTR---PQKGRIVLNGRvlFDAEKGIClppEKR-RIGYVFQDARLFPHyKVRGNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 455 RYGrLDASDEEVINAAKAASAhsfIKHLPNQYEtkiasegSNLSQGQKQLLAIARAILADADILILDEATSNIDT-RTel 533
Cdd:PRK11144 98 RYG-MAKSMVAQFDKIVALLG---IEPLLDRYP-------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLpRK-- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1267510758 534 qiQEGLNNLMRGRTSFVI-----AHRLKTIEK-ADQILVIKDGSIIEKGNHES 580
Cdd:PRK11144 165 --RELLPYLERLAREINIpilyvSHSLDEILRlADRVVVLEQGKVKAFGPLEE 215
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
47-330 |
6.73e-12 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 66.48 E-value: 6.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 47 IFLVFVTTLLGLLGPYLMGVIIDQyiVPKDLSGTARMCLLLIAIYGVTVFLT----WLQIFVMVNVALKTIQKIRQDIFE 122
Cdd:cd18560 2 LLLLILGKACNVLAPLFLGRAVNA--LTLAKVKDLESAVTLILLYALLRFSSkllkELRSLLYRRVQQNAYRELSLKTFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIA-MFALDWILAIVTLITVPIMFFVTKKL 201
Cdd:cd18560 80 HLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVfAFHFGAWLALIVFLSVLLYGVFTIKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 202 VAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGL 281
Cdd:cd18560 160 TEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGLTL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1267510758 282 VIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAG 330
Cdd:cd18560 240 GLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLTD 288
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
361-583 |
7.54e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.96 E-value: 7.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 361 ALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVL 440
Cdd:PRK10575 13 ALRNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 441 QDTYLFAGTIMDNI----RY------GRLDASDEEVINAAKAASAhsfIKHLPNQYEtkiasegSNLSQGQKQLLAIARA 510
Cdd:PRK10575 92 QQLPAAEGMTVRELvaigRYpwhgalGRFGAADREKVEEAISLVG---LKPLAHRLV-------DSLSGGERQRAWIAML 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267510758 511 ILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAhRLKTIEKA----DQILVIKDGSIIEKGNHESLME 583
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPAELMR 237
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
338-571 |
1.15e-11 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 64.76 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 338 MDEVPEIKNKKDAFVVQNLQGhvalenvsfgyeenKTI--LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQG 415
Cdd:COG4778 1 MTTLLEVENLSKTFTLHLQGG--------------KRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 416 QIHIDGKN-------IKEYDINSLR-GKIGVVLQdtylFAGTIMdniRYGRLD----------ASDEEVINAAKAASAHS 477
Cdd:COG4778 67 SILVRHDGgwvdlaqASPREILALRrRTIGYVSQ----FLRVIP---RVSALDvvaepllergVDREEARARARELLARL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 478 FIK----HLPNqyetkiasegSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFV-IA 552
Cdd:COG4778 140 NLPerlwDLPP----------ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIF 209
|
250 260
....*....|....*....|
gi 1267510758 553 HRLKTIEK-ADQILVIKDGS 571
Cdd:COG4778 210 HDEEVREAvADRVVDVTPFS 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
373-589 |
1.91e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 64.28 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 373 KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDIN--SLRGkIGVVLQDTYLFAG-T 449
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHkrARLG-IGYLPQEASIFRKlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 450 IMDNI-------------RYGRLDASDEEvinaakaasahsF-IKHLPNQYetkiaseGSNLSQGQKQLLAIARAILADA 515
Cdd:COG1137 95 VEDNIlavlelrklskkeREERLEELLEE------------FgITHLRKSK-------AYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 516 DILILDEATSNIDTRTELQIQEGLNNL-MRGrtsfvIA-----HR----LKTIEKAdqiLVIKDGSIIEKGNHESLMED- 584
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLkERG-----IGvlitdHNvretLGICDRA---YIISEGKVLAEGTPEEILNNp 227
|
....*..
gi 1267510758 585 --RGFYF 589
Cdd:COG1137 228 lvRKVYL 234
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
378-576 |
2.32e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.56 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 378 EVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSL---------RGKIGVVLQDTylfag 448
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHP----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 449 tiMDNIR--------------------YGRL--DASD--EEV-INAAKaasahsfIKHLPNQYetkiasegsnlSQGQKQ 503
Cdd:PRK11701 99 --RDGLRmqvsaggnigerlmavgarhYGDIraTAGDwlERVeIDAAR-------IDDLPTTF-----------SGGMQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 504 LLAIARAILADADILILDEATSNIDtrteLQIQEGLNNLMRGRTS------FVIAH-----RLktieKADQILVIKDGSI 572
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLD----VSVQARLLDLLRGLVRelglavVIVTHdlavaRL----LAHRLLVMKQGRV 230
|
....
gi 1267510758 573 IEKG 576
Cdd:PRK11701 231 VESG 234
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
360-572 |
2.42e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 64.31 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIhIDGKNikeyDINSLRGKIGVV 439
Cdd:PRK11247 13 LLLNAVSKRYGER-TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTA----PLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQDTYLFA-GTIMDNIRYG-----RLDAsdEEVINAAKAASAhsfikhlpnqyetkiASE-GSNLSQGQKQLLAIARAIL 512
Cdd:PRK11247 87 FQDARLLPwKKVIDNVGLGlkgqwRDAA--LQALAAVGLADR---------------ANEwPAALSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267510758 513 ADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRL-KTIEKADQILVIKDGSI 572
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
40-334 |
2.83e-11 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 64.80 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 40 KAALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGtarMCLLLIAIYGVTVF---LTWLQIFVMVNVALKTIQKI 116
Cdd:cd18569 1 RSALLFVVLAGLLLVIPGLVIPVFSRIFIDDILVGGLPDW---LRPLLLGMALTALLqglLTWLQQYYLLRLETKLALSS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 117 RQDIFEKIQTLSLRFFDVRSQGDLMSRVtndidnlnqALTQSVVQIISSAL--TFIGVT------IAMFALDWILAIVTL 188
Cdd:cd18569 78 SSRFFWHVLRLPVEFFSQRYAGDIASRV---------QSNDRVANLLSGQLatTVLNLVmavfyaLLMLQYDVPLTLIGI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 189 ITVPIMFFVTKKLVAYSGKNFAKRQKDLGELNGfieeaitgadvTTLYGKEK-ETVQN-------FNK--------INEQ 252
Cdd:cd18569 149 AIALLNLLVLRLVSRKRVDLNRRLLQDSGKLTG-----------TTMSGLQMiETLKAsgaesdfFSRwagyqakvLNAQ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 253 LRVSATkadtfSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGE 332
Cdd:cd18569 218 QELGRT-----NQLLGALPTLLSALTNAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDME 292
|
..
gi 1267510758 333 RV 334
Cdd:cd18569 293 RL 294
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
360-583 |
4.74e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.21 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLL--TRFYDIQQGQI-----------HID------ 420
Cdd:TIGR03269 1 IEVKNLTKKFD-GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgYVErpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 421 ------GKNIKEYDIN----------SLRGKIGVVLQDTYLFAG--TIMDNIrygrLDASDEEVINAAKAAS-AHSFIKH 481
Cdd:TIGR03269 80 epcpvcGGTLEPEEVDfwnlsdklrrRIRKRIAIMLQRTFALYGddTVLDNV----LEALEEIGYEGKEAVGrAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 482 LpnQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTIE 559
Cdd:TIGR03269 156 V--QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIE 233
|
250 260
....*....|....*....|....*
gi 1267510758 560 K-ADQILVIKDGSIIEKGNHESLME 583
Cdd:TIGR03269 234 DlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
371-570 |
4.82e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 62.26 E-value: 4.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 371 ENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYD--IQQGQIHIDGKNIKEydinSLRGKIGVVLQ-DTYLFA 447
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDK----NFQRSTGYVEQqDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 448 GTIMDNIRYgrldasdeevinaakaaSAhsfikhlpnqyetkiASEGsnLSQGQKQLLAIARAILADADILILDEATSNI 527
Cdd:cd03232 94 LTVREALRF-----------------SA---------------LLRG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1267510758 528 DTRTELQIQEGLNNL-MRGRTSFVIAHR--LKTIEKADQILVIKDG 570
Cdd:cd03232 140 DSQAAYNIVRFLKKLaDSGQAILCTIHQpsASIFEKFDRLLLLKRG 185
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
358-528 |
6.75e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.65 E-value: 6.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 358 GHVALE--NVSfgyeeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikEYDINSLRGK 435
Cdd:COG1129 253 GEVVLEveGLS-----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGK---PVRIRSPRDA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 436 I--GVVL-----QDTYLFAG-TIMDNI---------RYGRLDASDEEvinaakaASAHSFIKhlpnQYETKIASEG---S 495
Cdd:COG1129 325 IraGIAYvpedrKGEGLVLDlSIRENItlasldrlsRGGLLDRRRER-------ALAEEYIK----RLRIKTPSPEqpvG 393
|
170 180 190
....*....|....*....|....*....|...
gi 1267510758 496 NLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:COG1129 394 NLSGGNQQKVVLAKWLATDPKVLILDEPTRGID 426
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
376-577 |
8.89e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.88 E-value: 8.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVLQD--TYLFA----GT 449
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDpsTSLNPrqriSQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 450 IMD-NIRYG-RLDASD-EEVINAAKAAsahsfIKHLP---NQYETKIASegsnlsqGQKQLLAIARAILADADILILDEA 523
Cdd:PRK15112 109 ILDfPLRLNtDLEPEQrEKQIIETLRQ-----VGLLPdhaSYYPHMLAP-------GQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267510758 524 TSNIDTRT---------ELQIQEGLNNLmrgrtsFVIAHRLKTIEKADQILVIKDGSIIEKGN 577
Cdd:PRK15112 177 LASLDMSMrsqlinlmlELQEKQGISYI------YVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
42-334 |
9.13e-11 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 63.13 E-value: 9.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 42 ALTFVIFLVFVTTLLgllgPYLMGVIID----QYIVPKDLSGTARMCLLLIaiyGVTVFLTWLQIFVMVNVAlKTIQKIR 117
Cdd:cd18590 1 AFLFLTLAVICETFI----PYYTGRVIDilggEYQHNAFTSAIGLMCLFSL---GSSLSAGLRGGLFMCTLS-RLNLRLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 118 QDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFV 197
Cdd:cd18590 73 HQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 198 TKKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNL 277
Cdd:cd18590 153 QKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLG 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1267510758 278 GMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18590 233 VQVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
40-325 |
1.14e-10 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 62.95 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 40 KAALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGtarMCLLLIAIYGVTVF---LTWLQIFVMVNVALKTIQKI 116
Cdd:cd18779 1 PGLLGQILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDL---LGVLGLGLAALVLTqllAGLLRSHLLLRLRTRLDTQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 117 RQDIFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTL----ITVP 192
Cdd:cd18779 78 TLGFLEHLLRLPYRFFQQRSTGDLLMRL-SSNATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLglaaLQVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 193 IMFFVTKKLVAYSGKNFAKRqkdlGELNGFIEEAITGADVTTLYGKEKETVQNF-NKINEQLRVSATKAdTFSAFIFPSM 271
Cdd:cd18779 157 LLLATRRRVRELMARELAAQ----AEAQSYLVEALSGIETLKASGAEDRALDRWsNLFVDQLNASLRRG-RLDALVDALL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1267510758 272 NFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLsqfATLMNTIQ 325
Cdd:cd18779 232 ATLRLAAPLVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPL---ASLVGTAQ 282
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
374-528 |
1.17e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 61.22 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 374 TILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeyDINSLRGKigvvLQDTYLFAG----- 448
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT-----PLAEQRDE----PHENILYLGhlpgl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 449 ----TIMDNIR-YGRLDASDEEVINAAKAASAHSFIKHLPNQYetkiasegsnLSQGQKQLLAIARAILADADILILDEA 523
Cdd:TIGR01189 85 kpelSALENLHfWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQ----------LSAGQQRRLALARLWLSRRPLWILDEP 154
|
....*
gi 1267510758 524 TSNID 528
Cdd:TIGR01189 155 TTALD 159
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
373-547 |
1.26e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 61.35 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 373 KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSLRGKIGVVLQDTYLFAGTIMD 452
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 453 NIRYGRLDASDEEVINAAKAASAHSFiKHLPNQYetkiasegsnLSQGQKQLLAIARAILADADILILDEATSNIDTRTE 532
Cdd:cd03231 93 NLRFWHADHSDEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170
....*....|....*
gi 1267510758 533 LQIQEglnnLMRGRT 547
Cdd:cd03231 162 ARFAE----AMAGHC 172
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
360-544 |
1.78e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.94 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeyDINSL----RGk 435
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGR-----VVNELepadRD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 436 IGVVLQDTYLFAG-TIMDNIRYG----RLDAS--DEEVINAAKAASAHSFIKHLPNQyetkiasegsnLSQGQKQLLAIA 508
Cdd:PRK11650 78 IAMVFQNYALYPHmSVRENMAYGlkirGMPKAeiEERVAEAARILELEPLLDRKPRE-----------LSGGQRQRVAMG 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 1267510758 509 RAILADADILILDEATSNIDTRteLQIQeglnnlMR 544
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDAK--LRVQ------MR 174
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
110-303 |
3.43e-10 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 61.34 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 110 LKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLI 189
Cdd:cd18585 64 FRLLSNLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 190 TVPIMFFVTKKLVAYSGKNFAKRQKDL-GELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRVSATKADTFSAFIF 268
Cdd:cd18585 144 GLLLAGVVIPLLFYRLGKKIGQQLVQLrAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQ 223
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1267510758 269 PSMNFINNLGMGLVIGTGSVMVLNG--------MTTVGVIAAF 303
Cdd:cd18585 224 ALMILLSGLTVWLVLWLGAPLVQNGaldgallaMLVFAVLASF 266
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
376-573 |
3.60e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.44 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI-----KEydinSLRGKIGVVLQDTYLFAG-T 449
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkssKE----ALENGISMVHQELNLVLQrS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 450 IMDNIRYGR-----LDASDEEVINAAKAASAHSFIKHLPNQyetKIAsegsNLSQGQKQLLAIARAILADADILILDEAT 524
Cdd:PRK10982 90 VMDNMWLGRyptkgMFVDQDKMYRDTKAIFDELDIDIDPRA---KVA----TLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1267510758 525 SNIdTRTELQ----IQEGLNNlmRGRTSFVIAHRLKTIEK-ADQILVIKDGSII 573
Cdd:PRK10982 163 SSL-TEKEVNhlftIIRKLKE--RGCGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
362-533 |
4.05e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 362 LENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIdgknikeydinslrG-KIGVVL 440
Cdd:PRK11147 322 MENVNYQIDG-KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC--------------GtKLEVAY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 441 QDTYLFA----GTIMDNIRYGRldasdEEV-INAAKaasAH------SFIKHlPNQYETKIASegsnLSQGQKQLLAIAR 509
Cdd:PRK11147 387 FDQHRAEldpeKTVMDNLAEGK-----QEVmVNGRP---RHvlgylqDFLFH-PKRAMTPVKA----LSGGERNRLLLAR 453
|
170 180
....*....|....*....|....*
gi 1267510758 510 AILADADILILDEATSNIDTRT-EL 533
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLDVETlEL 478
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
375-584 |
4.60e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.38 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 375 ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINsLRGKIGVVL--QDTYLFAG-TIM 451
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIYLvpQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 452 DNIRYGRLDASDEEVINAAKAASAHSfikHLpnqyetKIASEGSNLSQGQKQLLAIARAILADADILILDEATSN---ID 528
Cdd:PRK15439 105 ENILFGLPKRQASMQKMKQLLAALGC---QL------DLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASltpAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 529 TRTEL-QIQEGLNnlmRGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESLMED 584
Cdd:PRK15439 176 TERLFsRIRELLA---QGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTD 230
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
40-327 |
5.13e-10 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 60.99 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 40 KAALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQD 119
Cdd:cd18783 1 KRLFRDVAIASLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 120 IFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTL-----ITVPIM 194
Cdd:cd18783 81 TFDRLLSLPIDFFERTPAGVLTKHM-QQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLafsalIALIIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 195 FFVtkklvaysgKNFAKRQKDL----GELNGFIEEAITGAD-VTTLyGKEKETVQNFNKINEQLRVSATKADTFSAFIFP 269
Cdd:cd18783 160 AFL---------PPFRRRLQALyraeGERQAFLVETVHGIRtVKSL-ALEPRQRREWDERVARAIRARFAVGRLSNWPQT 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 270 SMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAA 327
Cdd:cd18783 230 LTGPLEKLMTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEA 287
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
45-214 |
7.91e-10 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 60.19 E-value: 7.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 45 FVIFLVFVTTLLGLLGPYLMGVIIdQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQ---------IFVMVNVALKTIqk 115
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLI-SYLSSYPDEPLSEGYLLALALFLVSLLQSLLLhqyfflsfrLGMRVRSALSSL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 116 irqdIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALtQSVVQIISSALTFIGVTIAMFA-LDW-ILA--IVTLITV 191
Cdd:cd18579 78 ----IYRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFF-LFLHYLWSAPLQIIVALYLLYRlLGWaALAglGVLLLLI 152
|
170 180
....*....|....*....|...
gi 1267510758 192 PIMFFVTKKLVAYSGKNFAKRQK 214
Cdd:cd18579 153 PLQAFLAKLISKLRKKLMKATDE 175
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
371-590 |
8.05e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.82 E-value: 8.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 371 ENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRfyDIQ----QGQIHIDGKNIKEydinSLRGKIGVVLQDTYLF 446
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG--RIQgnnfTGTILANNRKPTK----QILKRTGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 447 AG-TIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLP-NQYETKIASEG--SNLSQGQKQLLAIARAILADADILILDE 522
Cdd:PLN03211 153 PHlTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGlTKCENTIIGNSfiRGISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267510758 523 ATSNIDTRTELQIQEGLNNLM-RGRTSFVIAHR--LKTIEKADQILVIKDGSIIEKGNHESLMedrgFYFD 590
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAqKGKTIVTSMHQpsSRVYQMFDSVLVLSEGRCLFFGKGSDAM----AYFE 299
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
348-581 |
1.04e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.41 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 348 KDAFVVQNLqghvaleNVSFGYEENKT-ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDG----- 421
Cdd:PRK10261 10 RDVLAVENL-------NIAFMQEQQKIaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 422 KNIKEYDIN--------SLRG-KIGVVLQD-------TYLFAGTIMDNIRYGRlDASDEEVINAAK-------AASAHSF 478
Cdd:PRK10261 83 RSRQVIELSeqsaaqmrHVRGaDMAMIFQEpmtslnpVFTVGEQIAESIRLHQ-GASREEAMVEAKrmldqvrIPEAQTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 479 IKHLPNQyetkiasegsnLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFV--IAHRLK 556
Cdd:PRK10261 162 LSRYPHQ-----------LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVifITHDMG 230
|
250 260
....*....|....*....|....*.
gi 1267510758 557 TI-EKADQILVIKDGSIIEKGNHESL 581
Cdd:PRK10261 231 VVaEIADRVLVMYQGEAVETGSVEQI 256
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
86-263 |
1.69e-09 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 59.60 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 86 LLIAIYGVTVFLT-WLQIFVMVNVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIIS 164
Cdd:cd18558 63 YYYLIIGAIVLITaYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 165 SALTFIGVTIAMFALDWILAIVTLITVPIMFFV----TKKLVAYSGKNfakrQKDLGELNGFIEEAITGA-DVTTLYGKE 239
Cdd:cd18558 143 NIATFGTGFIIGFIRGWKLTLVILAISPVLGLSavvwAKILSGFTDKE----KKAYAKAGAVAEEVLEAFrTVIAFGGQQ 218
|
170 180
....*....|....*....|....
gi 1267510758 240 KETVQNFNKINEQLRVSATKADTF 263
Cdd:cd18558 219 KEETRYAQNLEIAKRNGIKKAITF 242
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
360-586 |
2.63e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.91 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 360 VALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTrfydiqqGQIHIDGKNIKEydinSLRGKIGVV 439
Cdd:PRK15064 320 LEVENLTKGFD-NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLV-------GELEPDSGTVKW----SENANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 440 LQD-TYLFAG--TIMDNIRYGRLDASDEEVINAAKAasahsfiKHLPNQYETKiaSEGSNLSQGQKQLLAIARAILADAD 516
Cdd:PRK15064 388 AQDhAYDFENdlTLFDWMSQWRQEGDDEQAVRGTLG-------RLLFSQDDIK--KSVKVLSGGEKGRMLFGKLMMQKPN 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267510758 517 ILILDEATSNIDtrteLQIQEGLNN---LMRGRTSFVIAHRLKTIEKADQILVIKDGSIIE-KGNHESLMEDRG 586
Cdd:PRK15064 459 VLVMDEPTNHMD----MESIESLNMaleKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDfSGTYEEYLRSQG 528
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
354-584 |
3.50e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.85 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 354 QNLQGHVALENVSFGyEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDINSL- 432
Cdd:PRK11831 2 QSVANLVDMRGVSFT-RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 433 --RGKIGVVLQDTYLFAG-TIMDNIRY-----GRLDAS--DEEVINAAKAASAHSFIKHLPnqyetkiasegSNLSQGQK 502
Cdd:PRK11831 81 tvRKRMSMLFQSGALFTDmNVFDNVAYplrehTQLPAPllHSTVMMKLEAVGLRGAAKLMP-----------SELSGGMA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 503 QLLAIARAILADADILILDEATSNIDTRTE---LQIQEGLNNLMrGRTSFVIAHRL-KTIEKADQILVIKDGSIIEKGNH 578
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDPITMgvlVKLISELNSAL-GVTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSA 228
|
....*.
gi 1267510758 579 ESLMED 584
Cdd:PRK11831 229 QALQAN 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
376-585 |
3.51e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.54 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 376 LKE-VSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIkeyDINSLRGKI--GVVL------QDTYLF 446
Cdd:PRK11288 268 LREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI---DIRSPRDAIraGIMLcpedrkAEGIIP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 447 AGTIMDNI---------RYGRLdasdeevINAAK-AASAHSFIKHL----PNQyETKIAsegsNLSQGQKQLLAIARAIL 512
Cdd:PRK11288 345 VHSVADNInisarrhhlRAGCL-------INNRWeAENADRFIRSLniktPSR-EQLIM----NLSGGNQQKAILGRWLS 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267510758 513 ADADILILDEATSNIDTRTELQIQEGLNNLM-RGRTSFVIAHRL-KTIEKADQILVIKDGSIIEKGNHESLMEDR 585
Cdd:PRK11288 413 EDMKVILLDEPTRGIDVGAKHEIYNVIYELAaQGVAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQATERQ 487
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
40-189 |
4.19e-09 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350015 [Multi-domain] Cd Length: 294 Bit Score: 58.22 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 40 KAALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLS-----GTARMCLLlIAIYGVTVFLTW--LQIFVMVNVALKT 112
Cdd:cd18571 1 KKLILQLLLGLLLGSLLQLIFPFLTQSIVDKGINNKDLNfiyliLIAQLVLF-LGSTSIEFIRSWilLHISSRINISIIS 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267510758 113 iqkirqDIFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLI 189
Cdd:cd18571 80 ------DFLIKLMRLPISFFDTKMTGDILQRI-NDHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIFLI 149
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
44-338 |
9.11e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 57.09 E-value: 9.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 44 TFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYG----VTVFLTWLQIFVMVNVALKTIQKIRQD 119
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVSVLYYLGIYAlislLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 120 IFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMFFVtk 199
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYI-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 200 klvaysGKNFAKRQKDLGELN--------GFIEEAITGadVTTL--YGKEKE-TVQNFNKINEQLRVSatkadtfsaFIF 268
Cdd:cd18604 160 ------GRLYLRASRELKRLEsvarspilSHFGETLAG--LVTIraFGAEERfIEEMLRRIDRYSRAF---------RYL 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267510758 269 PSMNF-----INNLGMGLVIGTGSVMVLNGMTTVGvIAAF-INYSRQFSRPLSQFATLMNTIQA---AVaggERVFEIM 338
Cdd:cd18604 223 WNLNRwlsvrIDLLGALFSFATAALLVYGPGIDAG-LAGFsLSFALGFSSAILWLVRSYNELELdmnSV---ERIQEYL 297
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
372-572 |
1.14e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.63 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 372 NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQ-QGQIHIDGKNIKeydINS----LRGKIGVVLQDTYLF 446
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVK---IRNpqqaIAQGIAMVPEDRKRD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 447 aG--TIMD---NIRYGRLDA-SDEEVIN-AAKAASAHSFIKHLpnqyETKIAS---EGSNLSQGQKQLLAIARAILADAD 516
Cdd:PRK13549 351 -GivPVMGvgkNITLAALDRfTGGSRIDdAAELKTILESIQRL----KVKTASpelAIARLSGGNQQKAVLAKCLLLNPK 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 517 ILILDEATSNIDTRTELQIQEGLNNLM-RGRTSFVIAHRLKTI-EKADQILVIKDGSI 572
Cdd:PRK13549 426 ILILDEPTRGIDVGAKYEIYKLINQLVqQGVAIIVISSELPEVlGLSDRVLVMHEGKL 483
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
385-575 |
1.19e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.30 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 385 PGETIALVGPTGSGKTTIINLLTRFYDIQQGQIH-IDGKNIKEYDINSLRGKIgvvlqdtylfagtimdnirygrldasd 463
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 464 eevinaakaasahsfikhlpnqyetkIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQE------ 537
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrl 107
|
170 180 190
....*....|....*....|....*....|....*...
gi 1267510758 538 GLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSIIEK 575
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLL 145
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
372-573 |
1.61e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.96 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 372 NKTILKEVSLKARPGETIALVGPTGSGKTTIINLL---TRFYDIQQGQIHIDGKNIKEyDINSLRGKIGVVLQDTYLFAG 448
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKE-FAEKYPGEIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 449 -TImdnirygrldasdEEVINAAKAASAHSFIKhlpnqyetkiasegsNLSQGQKQLLAIARAILADADILILDEATSNI 527
Cdd:cd03233 98 lTV-------------RETLDFALRCKGNEFVR---------------GISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1267510758 528 DTRTELQIQEGLNNLMR--GRTSFVIAHR--LKTIEKADQILVIKDGSII 573
Cdd:cd03233 150 DSSTALEILKCIRTMADvlKTTTFVSLYQasDEIYDLFDKVLVLYEGRQI 199
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
141-570 |
3.49e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 56.30 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 141 MSRVTNDIDNLNQALTQSVVQI-ISSALTFIGVTIAMfaLDWILAIVTLIT------VPIMF---FVTKKLVAYSGKNFA 210
Cdd:TIGR00954 187 VSNLDSRIQNPDQLLTQDVEKFcDSVVELYSNLTKPI--LDVILYSFKLLTalgsvgPAGLFaylFATGVVLTKLRPPIG 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 211 K----RQKDLGELNGFIEEAITGADVTTLYG---KEKETVQN-FNKINEQLRvsatKADTFSAfifpSMNFINNL----- 277
Cdd:TIGR00954 265 KltveEQALEGEYRYVHSRLIMNSEEIAFYQgnkVEKETVMSsFYRLVEHLN----LIIKFRF----SYGFLDNIvakyt 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 278 --GMGLVIGTGSVMVLNGMTTVG-----VIAAFINYSR---QFSRPLSQFATLMNTIQAAVAGGERVFEIMDEVPEIK-- 345
Cdd:TIGR00954 337 wsAVGLVAVSIPIFDKTHPAFLEmseeeLMQEFYNNGRlllKAADALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVKsg 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 346 NKKDAFVVQNLQGH---------------------VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIIN 404
Cdd:TIGR00954 417 NFKRPRVEEIESGReggrnsnlvpgrgiveyqdngIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFR 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 405 LLTRFYDIQQGQIHIDGKnikeydinslrGKIGVVLQDTYLFAGTIMDNIRYGrlDASDEEVinaAKAASAHSFIKHLPN 484
Cdd:TIGR00954 497 ILGELWPVYGGRLTKPAK-----------GKLFYVPQRPYMTLGTLRDQIIYP--DSSEDMK---RRGLSDKDLEQILDN 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 485 QYETKIASEGSN----------LSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLmrGRTSFVIAHR 554
Cdd:TIGR00954 561 VQLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHR 638
|
490
....*....|....*.
gi 1267510758 555 lKTIEKADQILVIKDG 570
Cdd:TIGR00954 639 -KSLWKYHEYLLYMDG 653
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
332-584 |
5.22e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 55.58 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 332 ERVFEIMDEVPEIKNKKDAFVVQNLqghVALENVSFGY-EENKTILKEV---SLKARPGETIALVGPTGSGKTTIINLLT 407
Cdd:TIGR03269 255 EVVAVFMEGVSEVEKECEVEVGEPI---IKVRNVSKRYiSVDRGVVKAVdnvSLEVKEGEIFGIVGTSGAGKTTLSKIIA 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 408 RFYDIQQGQIHI----DGKNIKEYDINsLRGK----IGVVLQDTYLFA-GTIMDNIRYG-RLDASDE----EVINAAKAA 473
Cdd:TIGR03269 332 GVLEPTSGEVNVrvgdEWVDMTKPGPD-GRGRakryIGILHQEYDLYPhRTVLDNLTEAiGLELPDElarmKAVITLKMV 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 474 S-----AHSFIKHLPNQyetkiasegsnLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMR--GR 546
Cdd:TIGR03269 411 GfdeekAEEILDKYPDE-----------LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQ 479
|
250 260 270
....*....|....*....|....*....|....*....
gi 1267510758 547 TSFVIAHRLKTI-EKADQILVIKDGSIIEKGNHESLMED 584
Cdd:TIGR03269 480 TFIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
378-572 |
5.54e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 55.60 E-value: 5.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 378 EVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQ-QGQIHIDGKNIkeyDI----NSLRGKIGVVLQDTYLfAGTIMD 452
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPV---DIrnpaQAIRAGIAMVPEDRKR-HGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 453 -----NIRYGRLDA-SDEEVINAAKAASAhsfIKHLPNQYETKIASEG---SNLSQGQKQLLAIARAILADADILILDEA 523
Cdd:TIGR02633 354 lgvgkNITLSVLKSfCFKMRIDAAAELQI---IGSAIQRLKVKTASPFlpiGRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1267510758 524 TSNIDTRTELQIQEGLNNLM-RGRTSFVIAHRL-KTIEKADQILVIKDGSI 572
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAqEGVAIIVVSSELaEVLGLSDRVLVIGEGKL 481
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
382-566 |
6.30e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.56 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 382 KARPGETIALVGPTGSGKTTIINLLTrfydiqqGQIHIDGKNIKEyDInslrgKIGVVLQdtYL---FAGTIMDNIRygr 458
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILA-------GVLKPDEGEVDE-DL-----KISYKPQ--YIspdYDGTVEEFLR--- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 459 ldasdeeviNAAKAASAHSFIKH-------LPNQYETKIasegSNLSQGQKQLLAIARAILADADILILDEATSNIDTRT 531
Cdd:COG1245 424 ---------SANTDDFGSSYYKTeiikplgLEKLLDKNV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 490
|
170 180 190
....*....|....*....|....*....|....*...
gi 1267510758 532 ELQIQEGLNNLM--RGRTSFVIAHRLKTIEK-ADQILV 566
Cdd:COG1245 491 RLAVAKAIRRFAenRGKTAMVVDHDIYLIDYiSDRLMV 528
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
378-529 |
7.24e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.88 E-value: 7.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 378 EVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKeydinslrgKIGVVLQDTYLFAG--------- 448
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR---------RQRDEYHQDLLYLGhqpgiktel 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 449 TIMDNIR-YGRL--DASDEEVINAAKAASAHSFiKHLPnqyetkiaseGSNLSQGQKQLLAIARAILADADILILDEATS 525
Cdd:PRK13538 90 TALENLRfYQRLhgPGDDEALWEALAQVGLAGF-EDVP----------VRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
....
gi 1267510758 526 NIDT 529
Cdd:PRK13538 159 AIDK 162
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
384-567 |
9.78e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 9.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 384 RPGETIALVGPTGSGKTTIINLLTrfydiqqGQI------------------HIDGKNIKEYdINSLR-GKIGVVLQDTY 444
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKILS-------GELipnlgdyeeepswdevlkRFRGTELQNY-FKKLYnGEIKVVHKPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 445 L------FAGTIMDNIR----YGRLDasdeEVINAAKaasahsfIKHLPNQyetkiasEGSNLSQGQKQLLAIARAILAD 514
Cdd:PRK13409 169 VdlipkvFKGKVRELLKkvdeRGKLD----EVVERLG-------LENILDR-------DISELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1267510758 515 ADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVIAHRLKTIEK-ADQILVI 567
Cdd:PRK13409 231 ADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
364-528 |
1.44e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.17 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 364 NVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINlltrfydIQQGqihIDgkniKEYDINSLRG---KIGVVL 440
Cdd:TIGR03719 9 RVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------IMAG---VD----KDFNGEARPQpgiKVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 441 QDTYLFAG-TIMDNIRYG---RLDASDE-EVINAAKAASAHSFIKHLPNQ--YETKIASEG------------------- 494
Cdd:TIGR03719 75 QEPQLDPTkTVRENVEEGvaeIKDALDRfNEISAKYAEPDADFDKLAAEQaeLQEIIDAADawdldsqleiamdalrcpp 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1267510758 495 -----SNLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:TIGR03719 155 wdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
371-570 |
1.56e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 371 ENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYD---IQQGQIHIDGKNIKEydinSLRGKIGVVLQ-DTYLF 446
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLDS----SFQRSIGYVQQqDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 447 AGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLP-NQY-ETKIASEGSNLSQGQKQLLAIARAILADADILI-LDEA 523
Cdd:TIGR00956 850 TSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEmESYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEP 929
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1267510758 524 TSNIDTRTELQIQEGLNNLMR-GRTSFVIAHRLKTI--EKADQILVIKDG 570
Cdd:TIGR00956 930 TSGLDSQTAWSICKLMRKLADhGQAILCTIHQPSAIlfEEFDRLLLLQKG 979
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
384-567 |
2.15e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.02 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 384 RPGETIALVGPTGSGKTTIINLLTrfydiqqGQI------------------HIDGKNIKEYdINSLR-GKIGVVLQDTY 444
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILS-------GELkpnlgdydeepswdevlkRFRGTELQDY-FKKLAnGEIKVAHKPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 445 ------LFAGTIMDnirygRLDASDE-----EVINAAKaasahsfIKHLPNQyetkiasEGSNLSQGQKQLLAIARAILA 513
Cdd:COG1245 169 vdlipkVFKGTVRE-----LLEKVDErgkldELAEKLG-------LENILDR-------DISELSGGELQRVAIAAALLR 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1267510758 514 DADILILDEATSNIDTRTELQIQEGLNNLMR-GRTSFVIAHRLKTIEK-ADQILVI 567
Cdd:COG1245 230 DADFYFFDEPSSYLDIYQRLNVARLIRELAEeGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
385-528 |
2.49e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.77 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 385 PGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDIN---SLRGKIGVVLQDTylfagTIMDNIRYgrlda 461
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSrfmAYLGHLPGLKADL-----STLENLHF----- 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267510758 462 sdeevINAAKAASAhsfiKHLPNQYETKIASEG------SNLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:PRK13543 106 -----LCGLHGRRA----KQMPGSALAIVGLAGyedtlvRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
369-566 |
3.02e-07 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 52.03 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 369 YEENKTILKEVSLKARPG-----ETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIkEYDINSLRGKIGVVLQDt 443
Cdd:cd03237 3 YPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKADYEGTVRD- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 444 ylFAGTIMDNirYGRLDASDEEVINaakaasahsfikhlPNQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEA 523
Cdd:cd03237 81 --LLSSITKD--FYTHPYFKTEIAK--------------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1267510758 524 TSNIDTRTELQIQEGLNNLM--RGRTSFVIAHRLKTIEK-ADQILV 566
Cdd:cd03237 143 SAYLDVEQRLMASKVIRRFAenNEKTAFVVEHDIIMIDYlADRLIV 188
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
383-566 |
4.56e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 383 ARPGETIALVGPTGSGKTTIINLLTrfydiqqGQIHIDGKNIkEYDInslrgKIGVVLQdtYL---FAGTIMDNIRygrl 459
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLA-------GVLKPDEGEV-DPEL-----KISYKPQ--YIkpdYDGTVEDLLR---- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 460 dasdeevinAAKAASAHSFIKH-------LPNQYETKIasegSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTE 532
Cdd:PRK13409 423 ---------SITDDLGSSYYKSeiikplqLERLLDKNV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 489
|
170 180 190
....*....|....*....|....*....|....*..
gi 1267510758 533 LQIQEGLNNLMRGR--TSFVIAHRLKTIEK-ADQILV 566
Cdd:PRK13409 490 LAVAKAIRRIAEEReaTALVVDHDIYMIDYiSDRLMV 526
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
335-574 |
9.79e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.71 E-value: 9.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 335 FEIMDEVPEIKNKKDAFVVQNLQGHvalenvsfgyeENKTIlKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQ 414
Cdd:PRK09700 250 FNAMKENVSNLAHETVFEVRNVTSR-----------DRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAG 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 415 GQIHIDGKNIK---EYDinSLRGKIGVVLQ---DTYLFAG-TIMDNIR-------------YGRLDASDEEVInaAKAAS 474
Cdd:PRK09700 318 GEIRLNGKDISprsPLD--AVKKGMAYITEsrrDNGFFPNfSIAQNMAisrslkdggykgaMGLFHEVDEQRT--AENQR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 475 AHSFIK-HLPNQYETKiasegsnLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEglnnLMR-----GRTS 548
Cdd:PRK09700 394 ELLALKcHSVNQNITE-------LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYK----VMRqladdGKVI 462
|
250 260
....*....|....*....|....*..
gi 1267510758 549 FVIAHRLKTI-EKADQILVIKDGSIIE 574
Cdd:PRK09700 463 LMVSSELPEIiTVCDRIAVFCEGRLTQ 489
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
384-555 |
1.73e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 49.67 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 384 RPGETIALVGPTGSGKTTIINLLT--------RFYDIQQGQIHID---GKNIKEYDINSLRGKIGVVLQDTYL------F 446
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVIVKPQYVdlipkaV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 447 AGTIMDNirygrLDASDE-----EVINAAKaasahsfIKHLPNQyetkiasEGSNLSQGQKQLLAIARAILADADILILD 521
Cdd:cd03236 104 KGKVGEL-----LKKKDErgkldELVDQLE-------LRHVLDR-------NIDQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190
....*....|....*....|....*....|....*
gi 1267510758 522 EATSNIDTRTELQIQEGLNNLMR-GRTSFVIAHRL 555
Cdd:cd03236 165 EPSSYLDIKQRLNAARLIRELAEdDNYVLVVEHDL 199
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
340-524 |
2.07e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.41 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 340 EVPEIKNKKDAfvvqnLQGHVALE--NVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQI 417
Cdd:COG3845 241 EVLLRVEKAPA-----EPGEVVLEveNLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSI 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 418 HIDGKNIKEYDINSLRGK-IGVVLQDTY---LFAG-TIMDNI---RYGRLDASDEEVINAAKaasAHSFIKHLPNQYETK 489
Cdd:COG3845 316 RLDGEDITGLSPRERRRLgVAYIPEDRLgrgLVPDmSVAENLilgRYRRPPFSRGGFLDRKA---IRAFAEELIEEFDVR 392
|
170 180 190
....*....|....*....|....*....|....*...
gi 1267510758 490 IASEG---SNLSQGQKQLLAIARAILADADILILDEAT 524
Cdd:COG3845 393 TPGPDtpaRSLSGGNQQKVILARELSRDPKLLIAAQPT 430
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
364-562 |
3.90e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.02 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 364 NVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEyDINSLRGKIGVVLQDT 443
Cdd:PRK13540 6 ELDFDYHD-QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 444 ----YLfagTIMDNIRYG-RLDASDEEVINAAKAASAHSFIkhlpnQYETKIasegsnLSQGQKQLLAIARAILADADIL 518
Cdd:PRK13540 84 ginpYL---TLRENCLYDiHFSPGAVGITELCRLFSLEHLI-----DYPCGL------LSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1267510758 519 ILDEATSNIDTRTELQIQEGLN-NLMRGRTSFVIAHRLKTIEKAD 562
Cdd:PRK13540 150 LLDEPLVALDELSLLTIITKIQeHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
358-528 |
4.13e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.40 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 358 GHVALE----NVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTI-INLLTRFY--DIQqGQIHIDGKNIkeyDIN 430
Cdd:NF040905 254 GEVVFEvknwTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYgrNIS-GTVFKDGKEV---DVS 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 431 SLRGKI--------------GVVLQDTylfagtIMDNIRYGRLDA-SDEEVINAAK-AASAHSFIKHL----PNQYEtki 490
Cdd:NF040905 330 TVSDAIdaglayvtedrkgyGLNLIDD------IKRNITLANLGKvSRRGVIDENEeIKVAEEYRKKMniktPSVFQ--- 400
|
170 180 190
....*....|....*....|....*....|....*...
gi 1267510758 491 asEGSNLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:NF040905 401 --KVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
357-563 |
5.52e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 357 QGHVALENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRfyDIQQ---------GQIHIDGKNIkeY 427
Cdd:PRK10938 258 EPRIVLNNGVVSYND-RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQgysndltlfGRRRGSGETI--W 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 428 DInslRGKIGVV---LQDTYLFAGTIMDNIRYGRLDAsdeevINAAKAASAHSfiKHLPNQYETKIASEGS-------NL 497
Cdd:PRK10938 333 DI---KKHIGYVsssLHLDYRVSTSVRNVILSGFFDS-----IGIYQAVSDRQ--QKLAQQWLDILGIDKRtadapfhSL 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267510758 498 SQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMR-GRTS--FV----------IAHRLKTIEKADQ 563
Cdd:PRK10938 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISeGETQllFVshhaedapacITHRLEFVPDGDI 481
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
376-583 |
5.70e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 48.54 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTrfyDI---QQGQIHIDGKNIKEYDINSLRgKIGVV------------L 440
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLT---GIlvpTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrsqlwwdlpA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 441 QDTYLFAGTImdnirYgRLDASD-EEVINaakaasahSFIKHLpnQYETKIASEGSNLSQGQKQLLAIARAILADADILI 519
Cdd:COG4586 114 IDSFRLLKAI-----Y-RIPDAEyKKRLD--------ELVELL--DLGELLDTPVRQLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267510758 520 LDEATSNIDTRTELQIQEGLN--NLMRGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESLME 583
Cdd:COG4586 178 LDEPTIGLDVVSKEAIREFLKeyNRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
40-302 |
1.39e-05 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 47.21 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 40 KAALTFVIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQIFVMVNVALKTIQKIRQD 119
Cdd:cd18586 1 RRVFVEVGLFSFFINLLALAPPIFMLQVYDRVLPSGSLSTLLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 120 IFEKIQTLSLrffDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVTIAMFALDWILAIVTLITVPIMF---- 195
Cdd:cd18586 81 VFRAVLELPL---ESRPSGYWQQLL-RDLDTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVglaw 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 196 ---FVTKKLVAYSGKNFAKRqkdlgelNGFIEEAITGADVTTLYGKEKETVQNF-----NKINEQLRVSaTKADTFSAFI 267
Cdd:cd18586 157 lnhRATRKPLGEANEAQAAR-------DALAAETLRNAETIKALGMLGNLRRRWearhaETLELQIRAS-DLAGAISAIG 228
|
250 260 270
....*....|....*....|....*....|....*
gi 1267510758 268 FPSMNFINNlgmgLVIGTGSVMVLNGMTTVGVIAA 302
Cdd:cd18586 229 KTLRMALQS----LILGVGAYLVIDGELTIGALIA 259
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
376-582 |
2.97e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.92 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKE------------YdINSLRGKIGVVL--- 440
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTrspqdglangivY-ISEDRKRDGLVLgms 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 441 --QDTYLFAGTIMDNiRYGRLDASDEEvinaakaASAHSFIK----HLPNQyETKIAsegsNLSQGQKQLLAIARAILAD 514
Cdd:PRK10762 347 vkENMSLTALRYFSR-AGGSLKHADEQ-------QAVSDFIRlfniKTPSM-EQAIG----LLSGGNQQKVAIARGLMTR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 515 ADILILDEATSNIDTRTELQI--------QEGLNNLMrgrtsfVIAHRLKTIEKADQILVIKDGSI-----IEKGNHESL 581
Cdd:PRK10762 414 PKVLILDEPTRGVDVGAKKEIyqlinqfkAEGLSIIL------VSSEMPEVLGMSDRILVMHEGRIsgeftREQATQEKL 487
|
.
gi 1267510758 582 M 582
Cdd:PRK10762 488 M 488
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
360-425 |
4.67e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 4.67e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267510758 360 VALENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIdGKNIK 425
Cdd:PRK10636 313 LKMEKVSAGYGD-RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIK 376
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
496-570 |
6.61e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.14 E-value: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 496 NLSQGQKQL------LAIARAILADADILILDEATSNIDtrtELQIQEGLNNLMRGRTSF------VIAHRLKTIEKADQ 563
Cdd:cd03240 115 RCSGGEKVLasliirLALAETFGSNCGILALDEPTTNLD---EENIEESLAEIIEERKSQknfqliVITHDEELVDAADH 191
|
....*...
gi 1267510758 564 IL-VIKDG 570
Cdd:cd03240 192 IYrVEKDG 199
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
166-327 |
7.02e-05 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 45.12 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 166 ALTFIGVtIAMFAldWILAIVTLITVPIM----FFVTKKLVAYSGKNF-AKRQKdlgelNGFIEEAITGADVTTLYGKEK 240
Cdd:cd18587 128 VLLFLAV-IALIG--GPLALVPLVAIPLVllygLLLQKPLRRLVEESMrESAQK-----NALLVESLSGLETIKALGAEG 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 241 ETVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLVIGTGSVMVLNG-MTTVGVIAAFINYSRQFSrPLSQFAT 319
Cdd:cd18587 200 RMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQQLVTVAIVIVGVYLISDGeLTMGGLIACVILSGRALA-PLGQIAG 278
|
....*...
gi 1267510758 320 LMNTIQAA 327
Cdd:cd18587 279 LLTRYQQA 286
|
|
| ABC_6TM_ABCB6 |
cd18581 |
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ... |
47-327 |
1.02e-04 |
|
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350025 [Multi-domain] Cd Length: 300 Bit Score: 44.54 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 47 IFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTArMCLLLIAIYGVTVFL-----------TWLQIFVMVNVALKTIQK 115
Cdd:cd18581 2 LLLLAAGRVVNVLVPILYKKIVDSLTPDSADSPLA-FPWALILLYVFLKFLqgggsgsvgllSNLRSFLWIPVQQFTTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 116 IRQDIFEKIQTLSLRFFDVRSQGDL---MSRVTNDIDNLNQALTQSVV-QIISSAltfIGVTIAMFALDWILAIVTLITV 191
Cdd:cd18581 81 ISVKLFAHLHSLSLRWHLSRKTGEVlrvMDRGTSSINSLLSYVLFNIGpTIADII---IAIIYFAIAFNPWFGLIVFVTM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 192 PIMFFVTKKLVAYSGK--------NFAKRQKDLGELNGFieeaitgaDVTTLYGKEKETVQNFNKINEQLRVSATKADTF 263
Cdd:cd18581 158 ALYLILTIIITEWRTKfrremnklDNEKRAKAVDSLLNF--------ETVKYYNAERFEVERYRRAIDDYQVAEWKSNAS 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267510758 264 SAFIFPSMNFInnLGMGLVIGT--GSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAA 327
Cdd:cd18581 230 LNLLNTAQNLI--ITIGLLAGSllCAYFVVEGKLTVGDFVLFLTYIIQLYAPLNFFGTYYRMIQQS 293
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
88-196 |
1.19e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 44.39 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 88 IAIYG----VTVFLTWLQIFVMVNVALKTIQKIRQDIFEKIqtlsLR----FFDVRSQGDLMSRVTNDIDNLNQALTQSV 159
Cdd:cd18606 38 IGIYAglgvLQAIFLFLFGLLLAYLGIRASKRLHNKALKRV----LRapmsFFDTTPLGRILNRFSKDTDVLDNELPDSL 113
|
90 100 110
....*....|....*....|....*....|....*...
gi 1267510758 160 VQIISSALTFIGVTIAMFA-LDWILAIVtlitVPIMFF 196
Cdd:cd18606 114 RMFLYTLSSIIGTFILIIIyLPWFAIAL----PPLLVL 147
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
364-528 |
1.24e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.11 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 364 NVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINlltrfydIQQGqihIDgkniKEYDinslrG--------K 435
Cdd:PRK11819 11 RVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------IMAG---VD----KEFE-----GearpapgiK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 436 IGVVLQDTYLFAG-TIMDNIRYG---RLDASDE-EVINAAKAASAHSFIKHLPNQ--YETKIASEG-------------- 494
Cdd:PRK11819 72 VGYLPQEPQLDPEkTVRENVEEGvaeVKAALDRfNEIYAAYAEPDADFDALAAEQgeLQEIIDAADawdldsqleiamda 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1267510758 495 ----------SNLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:PRK11819 152 lrcppwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
88-254 |
1.43e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 44.01 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 88 IAIYG----VTVFLTWLQIFVMVNVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQII 163
Cdd:cd18603 44 LGVYGalglGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 164 SSALTFIG-VTIAMFALDWILAIVTLITVpIMFFVTKKLVAYSgknfakRQkdLGELNG--------FIEEAITGADVTT 234
Cdd:cd18603 124 NCLFQVIStLVVISISTPIFLVVIIPLAI-LYFFIQRFYVATS------RQ--LKRLESvsrspiysHFSETLQGASTIR 194
|
170 180
....*....|....*....|.
gi 1267510758 235 LYGKEKETV-QNFNKINEQLR 254
Cdd:cd18603 195 AYGVQERFIrESDRRVDENQR 215
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
372-570 |
4.02e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 372 NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDIN-SLRGKIGVVLQD---TYLFA 447
Cdd:PRK10982 260 RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANeAINHGFALVTEErrsTGIYA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 448 ------GTIMDNIR-----YGRLD----ASDEE-VINAAKAASAhsfikhlpnQYETKIASegsnLSQGQKQLLAIARAI 511
Cdd:PRK10982 340 yldigfNSLISNIRnyknkVGLLDnsrmKSDTQwVIDSMRVKTP---------GHRTQIGS----LSGGNQQKVIIGRWL 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267510758 512 LADADILILDEATSNIDTRTELQIQEGLNNLMRGRTSFVI--AHRLKTIEKADQILVIKDG 570
Cdd:PRK10982 407 LTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIisSEMPELLGITDRILVMSNG 467
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
336-401 |
5.83e-04 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 41.94 E-value: 5.83e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267510758 336 EIMDEVPEIKNKKDAfvVQNLQGHVAlENVSFGYEENkTILKEvslkarpGETIALVGPTGSGKTT 401
Cdd:TIGR03499 155 ELLEKLPEDADAEDA--WRWLREALE-GMLPVKPEED-PILEQ-------GGVIALVGPTGVGKTT 209
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
496-570 |
7.25e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.02 E-value: 7.25e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267510758 496 NLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNL-MRG-RTSFVIAHRLKTIEKADQILVIKDG 570
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLsEEGkKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
497-582 |
1.12e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.33 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 497 LSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGSII 573
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQTV 238
|
....*....
gi 1267510758 574 EKGNHESLM 582
Cdd:PRK15093 239 ETAPSKELV 247
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
389-572 |
1.78e-03 |
|
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.
Pssm-ID: 459814 [Multi-domain] Cd Length: 193 Bit Score: 39.83 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 389 IALVGPTGSGKTTIINLLTRFYdIQQGQihidgknikeydinslrgKIGVVLQDTYlfagtimdnirygRLDASDEEVIN 468
Cdd:pfam00448 3 ILLVGLQGSGKTTTIAKLAAYL-KKKGK------------------KVLLVAADTF-------------RAAAIEQLKQL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 469 AAKAASAhsFIKHLPNQYETKIASEgsnlsqgqkqllAIARAILADADILIldeatsnIDTRTELQIQEGLNNLMRgrts 548
Cdd:pfam00448 51 AEKLGVP--VFGSKTGADPAAVAFD------------AVEKAKAENYDVVL-------VDTAGRLQNDKNLMDELK---- 105
|
170 180
....*....|....*....|....
gi 1267510758 549 fviahRLKTIEKADQILVIKDGSI 572
Cdd:pfam00448 106 -----KIKRVVAPDEVLLVLDATT 124
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
336-403 |
3.08e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 40.26 E-value: 3.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 336 EIMDEVPEIKNKKDAFVVQNLQGHVAlenvsfgyeenKTILKEVSLKARPGETIALVGPTGSGKTTII 403
Cdd:PRK05703 182 KLLKLLLEHMPPRERTAWRYLLELLA-----------NMIPVRVEDILKQGGVVALVGPTGVGKTTTL 238
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
371-584 |
3.43e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.80 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 371 ENKTI--LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGkNIKEYDINS-LRGKIgvvlqdtylfa 447
Cdd:PRK13546 33 KNKTFfaLDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAISAgLSGQL----------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 448 gTIMDNIRYGRL---------DASDEEVINAAKAAsahSFIKHLPNQYetkiasegsnlSQGQKQLLAIARAILADADIL 518
Cdd:PRK13546 101 -TGIENIEFKMLcmgfkrkeiKAMTPKIIEFSELG---EFIYQPVKKY-----------SSGMRAKLGFSINITVNPDIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267510758 519 ILDEATSNID-TRTELQIQEGLNNLMRGRTSFVIAHRLKTIEK-ADQILVIKDGSIIEKGNHESLMED 584
Cdd:PRK13546 166 VIDEALSVGDqTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
88-200 |
4.71e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 39.61 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 88 IAIYGVTVFLTWL----QIFVMVNVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQII 163
Cdd:cd18601 62 LGIYAGLTAATFVfgflRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFL 141
|
90 100 110
....*....|....*....|....*....|....*...
gi 1267510758 164 SSALTFIGVTIAMFALD-WILaiVTLITVPIMFFVTKK 200
Cdd:cd18601 142 QLLLQVVGVVLLAVVVNpWVL--IPVIPLVILFLFLRR 177
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
388-429 |
5.69e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 36.83 E-value: 5.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1267510758 388 TIALVGPTGSGKTTIINLLTRFY-----------DIQQGQIHIDGKNIKEYDI 429
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKaivsdypgttrDPNEGRLELKGKQIILVDT 53
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
360-424 |
6.08e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 39.72 E-value: 6.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267510758 360 VALENVSFGYeeNKTI-LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI 424
Cdd:NF033858 2 ARLEGVSHRY--GKTVaLDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM 65
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
43-199 |
8.44e-03 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 38.39 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 43 LTFVIFLVFVTTLLGLLGPYLMGVIIDQyiVPKDLSGTARMCLLLIAIYGVTVFLTwlQIFVMVNVALKT------IQKI 116
Cdd:cd18556 4 FFSILFISLLSSILISISPVILAKITDL--LTSSSSDSYNYIVVLAALYVITISAT--KLLGFLSLYLQSslrvelIISI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 117 RQDIFEKIQTLSLRFFDVRSQGDLMSRV---TNDI----DNLNQALTQSVVQIISSaltfigVTIAMFALDWILAIVTLI 189
Cdd:cd18556 80 SSSYFRYLYEQPKTFFVKENSGDITQRLnqaSNDLytlvRNLSTNILPPLLQLIIA------IVVILSSGDYFVAALFLL 153
|
170
....*....|
gi 1267510758 190 TVpIMFFVTK 199
Cdd:cd18556 154 YA-VLFVINN 162
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
326-404 |
9.92e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.84 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267510758 326 AAVAGGERVFEimDEVPEIKNKKDAFVVQNLQGHVALENVSFGYEENKTI----------LKEVSLKARPGETIALVGPT 395
Cdd:TIGR00630 566 AGEHGGEVVAS--GTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNGKFltlkgarennLKNITVSIPLGLFTCITGVS 643
|
....*....
gi 1267510758 396 GSGKTTIIN 404
Cdd:TIGR00630 644 GSGKSTLIN 652
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